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tgt

Gene
Tgt
Protein
Queuine tRNA-ribosyltransferase catalytic subunit
Organism
Drosophila melanogaster
Length
427 amino acids
Function
Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product.
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
47.751 kDa
Sequence
MGPSHIPPLTYKVVAECSVSKARAGLMTLRHSEVNTPVFMPVGTQGTLKGIVPDQLIELNCQILLGNTYHLGLRPGIETLKKAGGLHKFMGWPRAILTDSGGFQMVSLLQLAEIDEHGVNFRSPFDNSQCMLTPEHSIEIQNAIGGDIMMQLDDVVKTTTTGPRVEEAMERTIRWVDRCIEAHARDDDQSLFPIVQGGLDVPLRQRCVSALMERQVRGFAVGGLSGGESKHDFWRMVDVCTGYLPKDKPRYLMGVGFAADLVVCVALGIDMFDCVFPTRTARFGCALVDSGQLNLKQPKYKLDMEPIDKDCDCSTCRRYTRSYLHHIATNESVSSSLLSIHNVAYQLRLMRSMREAIQRDEFPQFVADFMARHFKAEPVPAWIREALSAVNIQLPADPERIDEQDQKPKTEKRRETEDVAEEQVASS

Gene
tgt
Protein
Putative queuine tRNA-ribosyltransferase
Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Length
403 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
46.396 kDa
Sequence
MPLKFRIKHTLDRMRVGKVKTRHGSFETPVFIPVATLAAIRGLDNRDLKDMGVEVILANTYHLHLRPGDELIKELGGLHKFMNFDGVIVTDSGGFQAFSLGFGMEHGVGKIANNIFLEELREERLREAENERKKLAVVTDRGVRFKDPKSGRIVELTPKKSMEIQSNLGSDIIFAFDECTSPLSDRDYTEKALERTHRWAEECLQHYDRRQALFGVVQGGEYRDLREKSARFMAERDFAGYGIGGSLGKSKQDMLNILDWVIPLLPEEKPRHLLGIGAIEDLFNCTEKGVDMYDCVAPARWARRGHLYVSPAEGGNVRNKFRIHIKNAAFRIDNRPVDRTCDCLVCQNYSRAYLRHLYKANELLYFRLATYHNIYFVVKLMERIRESIADGSFYELKREWLGF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Roseiflexus sp. (strain RS-1)
Length
400 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
44.975 kDa
Sequence
MTLAFDIEARDPHSRARAGRITTAHGVIETPVFMPVGTRGSIKSLTPDEVRNHGAQIILGNTYHLYLQPGHELIARMGGLHHFMGWDGPILTDSGGFQVFSLVYGGIADEIKGRRPTQQVQPGMVKVTDDAVIFKSYIDGSMHVFTPERSIEIQKGIGADIILCFDELPPFHAGYDYTARSLERTHAWERRCLMFHRATQEGGLPFVPPNPYQALFGIVHGGVFPDLRRASAEYLRELPFDGLCIGGSLGENKQQMREVVDMTVPHMPDHLPRHLLGIGDVDDLIECVARGIDMFDCVSPTRLGRHGTALVRDAERRWKLNVANAALRDDPTPLDAWCDCYTCRRYSRAYIHHLFRAQELLGIRLVSLHNVAFLLKLMRTIRQSIIEGRFAHLRAEWLGI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Symbiobacterium thermophilum (strain T / IAM 14863)
Length
400 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
44.73 kDa
Sequence
MAVRWELLRRDPASAARLGRLHTPRGVIETPVFMPVGTQATVKTLNPEEVWDLGARIILSNTYHLYLRPGHDLVQEAGGLHRFMNWKGAVLTDSGGFQVFSLADLRKITEEGVQFRSHIDGSTHFLSPEKAIAVENALGADIIMAFDECTPWPCDYDYAKRSIERTARWAARCKAAHARPDEQALFGIVQGSTFADLRRQSAEEIVALDFPGYGIGGLSVGEPKELMHEMLEVQVPLLPDDRPRYLMGVGSPEDLVEGVWRGVDMFDCVLPTRIARHGTVFVPDGKMTVRNAEFARDFLPIQEGCDCYACRNFSRAYIRHLLKADEMLGLRLCSIHNLRFLVRLMEEIRAALAAGTFAEYRKAFLERWHAGEAERRERARAAGGAGHAPGPAEPLLPENR

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Polaromonas sp. (strain JS666 / ATCC BAA-500)
Length
398 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
44.333 kDa
Sequence
MLEFEVLKTDARTGEGANAHPGSHARRGQLTLTHGVVQTPIFMPVGTYGTVKGVMPQSLHEMGAQIILGNTFHLWMRPGLDVMKQFGGLHRFESWDKPILTDSGGFQVWSLGDMRKISEEGVKFASPVNGDKLFLTPEISMQIQTVLNSDIVMQFDECTPYDTKGHITTESEARSSMELSLRWAKRCVAEFDKLENPNALFGIVQGGMYQNLRHESLEALVELDLPGYAVGGVSVGEPKEEMQRIMAHTPHRLPADKPRYLMGVGTPEDLVEGVGAGIDMFDCVMPTRNARNGHLFTRFGDLKIRNARHKADEQPLDTTCTCYTCKGRTMPDGSTSGGFSRAYLHHLDRCGEMLGPMLASIHNLHYYLNLMQEIRDALDAGRFGEFAARFRTDRLRGV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Sorangium cellulosum (strain So ce56)
Length
394 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.171 kDa
Sequence
MSRTPGFSFSELARDGHARTGVLSTPHGDVLTPTFMPVGTQGSVKTLTPAEVAATGARIVLGNTYHLWLRPGPELVAQLGGLHAFTRWPHAMLTDSGGFQAFSLAERRTLVEDGFVFRSHLDGARKALTPEVAMEVQGLLGADIAMQLDVCPPGGAPRPEVEEACRLTTRWGKRCLAAKRPSQALFGIVQGGTSVALRMAHADELGALPFDGLALGGFSVGEPIAMMHEVVAQIGPHLDPTRPRYLMGVGTPIDLVHAIGAGVDMFDCVLPTRNARNGQALTQHGKIVIKQARYKEDRSPLDPTCACPTCTGGYSRAYLRHLYMAGEILVLRLLTEHNLHLYGRLMREARAAIAEGRYAAFARAWLGASDAGNANDANETVGATESTESTESTE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Length
394 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.851 kDa
Sequence
MNQCGTITAVFEFEIKQRDGRARTATFQTPRGAVTTPMFMPVGTQGTVKGISPQELLEIGSQMILANTYHLMLRPGEQLVKAHGGLPGFTAYPGPFLTDSGGFQVMSLGHMRKISEEGVVFKNHLDGSRVELTPERSIQVQEALGADVIMAFDECPPYPAERPYIEASLDRTVRWLERCHAVKTKDDQALFAIVQGGVHEDLRLKSLEATLPFATPGFAVGGLAVGESKEEMYPAVAFTAGRLPENKPRYLMGVGHPEDLVAGVALGIDMFDCVYPTRTGRFGYALTDDGRLNLNSSAPRTQLQPIDAECDCYACRHYTRAYLAHLLRAEEMLAPRMLSLHNLRYLHRLVERMRVAINGQQFHPWAADWSERYFHGNVPGWFTSAFERSTQSEI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95)
Length
392 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.59 kDa
Sequence
MNNFTYTLEHSDGEARAGQFSTPHGTIQTPVFMPVGTQATVKTLDPLEVEAIGSQIILSNTYHLYLRPSADLVAEMGGLHRFMQWPKPILTDSGGFQVFSLGPHSKIDEDGVTFKSHIDGSKHRFTPESAIGIQEKLGADIIMAFDECAPQPTTHAYTKAAMERTHRWLLRCIAAKTRADQALFGIVQGGVEADLRRESASFIAQQDVPGIGIGGLSVGEPKEQMYGMLEETTPLLPRNKPRYLMGVGSPEDLLEGVARGVDMFDCVLPTRLGRNGALFIPEGRLNIGNAKYAREDAPIDATCDCSTCQRFSRAYLRHLFRTEEVLGLRLATLHNLRFLIRLMEQAREAILQDRYQSFMDDWLSRFQTIPHAVREASRAARLNSLRTQGDKA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
Length
392 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.75 kDa
Sequence
MDKSFILNKTSPRSSARRGQLLTAHGQVETPVFCPVGSQATVKTLTPEDLKSVNVNMILSNTYHLYLRPGIPVVKEMGGLHKFMNWDGVILTDSGGYQIFSLANLRKLDEGGVSFRSHIDGSTRYITPEDAVSFQQDLGSDIAMVLDECPHSEASENEVLAAMERTHQWAKRCLAAHTLKSQHLFAIVQGGLSPVLRQQSAEYLASLDFPGYALGGLSLGEPKDITFETVRHTLRFLPENKPRYLMGVGAPEDLLEGVSCGVDIFDCVLPTRVARNGAFFSRLGRLNIRNASFATQKGPVDPECNCYTCRNYSAAYLHHLFRCEEILAYRLATIHNIAFLSNLMQEVRTSIEKDCFEEFKGDFLTRYQPTNESVRIEQKQKWLSARSGETSS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1)
Length
392 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.975 kDa
Sequence
MDKSFILNKTSSRSLARRGQLFTAHGKVETPVFCPVGSQATVKTLTPEDLKSVNINMILSNTYHLYLRPGIPIIKEMGGLHKFMNWDGVILTDSGGYQIFSLANLRKLDEGGVSFRSHIDGSTRYITPEDAVSFQQDLGSDIAMVLDECPHSEASENEVLAAMERTHQWAKRCLAAHTLKSQHLFAIVQGGLSPELRRQSAEYLASLDFPGYALGGLSLGEPKDITFETVRHTLRFLPENKPRYLMGVGAPEDLLEGVSCGVDIFDCVLPTRVARNGAFFSRLGRLNIRNAAFATQKGPIDPDCNCYTCRNYSAAYLHHLFRCEEILAYRLATIHNIAFLSNLMQEIRTSIEKDCFEEFKADFLSRYQPTNEAIRIEQKQKWLFGRNGEPPS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Dehalococcoides mccartyi (strain CBDB1)
Length
392 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
44.057 kDa
Sequence
MDKSFILNKTSSRSLARRGQLFTAHGKVETPVFCPVGSQAAVKTLTPEDLKSVNINMILSNTYHLYLRPGIPIIKEMGGLHKFMNWDEVILTDSGGYQIFSLANLRKLDEGGVSFRSHIDGSTRYITPEDAVSFQQDLGSDIAMVLDECPHSEASENEVLAAMERTHQWAKRCLAAHTLKIQHLFAIVQGGLSPELRRQSAEYLASLDFPGYALGGLSLGEPKDITFETVRHTLRFLPENKPRYLMGVGAPEDLLEGVSCGVDIFDCVLPTRVARNGAFFSRLGRLNIRNAAFATQKGPIDPECNCYTCRNYSAAYLHHLFRCEEILAYRLATIHNIAFLSNLMQEIRTSIEKDCFEEFKADFLSRYQPTNEAIRIEQKQKWLFGRNGEPPS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Acidovorax ebreus (strain TPSY)
Length
390 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.493 kDa
Sequence
MLKFEILATDTSSHARRGTLTLNHGVVQTPIFMPVGTYGTVKGVMPRSLREMGAQIILGNTFHLWMRPGLDVMQSFGGLHGFEQWDKPILTDSGGFQVWSLGSMRKITEEGVHFASPVNGDKLFMSPEVSMQIQTTLNSDIVMQLDECTPYETNGHKTTEAEARKSMEMSRRWAVRSKNEFERLGNPNALFGIVQGGMYKNLRQESLEALVEMDFPGYAVGGVSVGEPKDEMLDIMAHTPHRLPAHKPRYLMGVGTPEDLVEGVAQGVDMFDCVMPTRNARNGTLFTRYGDLKIRNARHKTDHQPLDPSCTCHACAGTEGVSWNDGGRGGFSRAYLHHLDRCGEMLGPMLTTIHNLHYYLNLMREVREALDAGQFGAFRARFKAERARGV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Acidovorax sp. (strain JS42)
Length
390 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.52 kDa
Sequence
MLKFEILATDTSSHARRGKLTLNHGVVQTPIFMPVGTYGTVKGVMPRSLREMGAQIILGNTFHLWMRPGLDVMQSFGGLHGFEQWDKPILTDSGGFQVWSLGSMRKITEEGVHFASPVNGDKLFMSPEVSMQIQTTLNSDIVMQLDECTPYETNGHKTTEAEARKSMEMSRRWAVRSKNEFERLGNPNALFGIVQGGMYKNLRQESLEALVEMDFPGYAVGGVSVGEPKDEMLDIMAHTPHRLPAHKPRYLMGVGTPEDLVEGVAQGVDMFDCVMPTRNARNGTLFTRYGDLKIRNARHKTDHQPLDPSCTCHACAGTEGVSWNDGGRGGFSRAYLHHLDRCGEMLGPMLTTIHNLHYYLNLMREVREALDAGQFGAFRARFKAERARGV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Verminephrobacter eiseniae (strain EF01-2)
Length
390 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.235 kDa
Sequence
MLQFDLLTTDPASHARRGRLTLRHGQVQTPIFMPVGTHGSVKGVLPRSLHEMGAQIILGNTFHLWLRPGLAVLQGFGGLHGFEKWNKPILTDSGGFQVWSLGALRTITEEGVHFASPVNGDKLFLSPEVSMQIQTTLDSDIVMQLDECTPYETRGQRTTERAACQSMQMSLRWAKRSQDEFQRLNNPNALFGIVQGGMYENLRAESLAALAAMDLPGYAIGGVSVGEPKDEMLRIMAHTPHRLPAHKPRYLMGVGTPEDLVEGVAQGVDMFDCVMPTRNARNGTLFTRFGDLKIRNARHKTDPQPLDGSCTCYTCAGPSGVAWDQGGRDGFSRAYLHHLERCGEMLGPMLSTVHNLHYYLNLMREIRQALDAGEFTQLRARLKADRARGV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Delftia acidovorans (strain DSM 14801 / SPH-1)
Length
390 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.545 kDa
Sequence
MLQFDLLKTDPSSHARRGQLTLNHGVVQTPIFMPVGTYGTVKGVMPRSLQEMGAQIILGNTFHLWMRPGLDIMQSFGGLHGFEKWDKPILTDSGGFQVWSLGAMRKITEEGVHFASPVNGDKLFMSPEVSMQIQTVLNSDIVMQLDECTPYETNGHKTTEAEARKSMEMSRRWAKRSSDEFQRLGNPNALFGIVQGGMYENLREESLQALVEMDFPGYAVGGVSVGEPKDEMLAIMAHTPHRLPAHKPRYLMGVGTPEDLVQGVADGVDMFDCVMPTRNARNGTIFTRYGDLKIRNARHKTDHQPLDPSCTCHACAGTSGVSWEQGGRDGFSRAYLHHLDRCGEMLGPMLTTIHNLHYYLNLMQEVRNALEAGNFTEMRARFKAERARGV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Acidovorax citrulli (strain AAC00-1)
Length
390 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.485 kDa
Sequence
MLQFELLATDPASHARRGTLTLNHGVVQTPIFMPVGTYGTVKGVMPRSLHEMGAQIILSNTFHLWMRPGLDVMQSFGGLHGFEQWNKPILTDSGGFQVWSLGAMRKITEEGVHFASPVNGDKLFMSPEVSMQIQTVLNSDIVMQLDECTPYETKGHKTTEAEARKSMEMSLRWARRSQDEFHRLGNPNALFGIVQGGMYKNLRQESLERLVEMDFPGYAVGGVSVGEPKDEMLDIMAHTPHRLPAHKPRYLMGVGTPEDLVQGVADGVDMFDCVMPTRNARNGTIFTRFGDLKIRNARHKADHQPLDPTCTCHACAGTEGVAWADGGRGGFSRAYLHHLDRCGEMLGPMLTTVHNLHYYLNLMREIRESLDAGRFGEFRARFAADRAQGV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6)
Length
390 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.549 kDa
Sequence
MLNFDLLTTEGHARRGRLTLNHGVVETPIFMPVGTYGTVKGVMPRDLETMGAQIILGNTFHLWMRPGQDVMAQFGGLHRFENWTRPILTDSGGFQVWSLGEMRKISEEGVRFASPVNGDKLFLTPEVSMQIQTVLNSDIVMQFDECTPYWQGAKNVGHITTEKEARVSMELSLRWAARSKAEFARLGNPNALFGIVQGGMFESLREESLNALVELDFPGYAVGGVSVGEPKDEMLRIMNHTPHLLPADKPRYLMGVGTPEDLVDGVACGVDMFDCVMPTRNARNGHLFTRYGDLKIRNARHKADERPLDETCSCQACKGSTLPDGRVTGGFSRAYLHHLDRCGEMLGPMLASIHNLHYYLNLMREVREALDAGRFEAFRAQFKADRARGV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12)
Length
388 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
45.186 kDa
Sequence
MSFEVIQRDKNTRARLGRLKTFHGEVNTPVFMPVGTQGAVKTLSPEEVEEVGAEIILSNTYHLFLRPGQEIIKKGGGLHRFIGWDKPILTDSGGYQVFSLARLRKIEEDGIYFNSHIDGSQYFFTPELVMEVQKALGSDIIMPLDICLGYGASYWETKEALEITLRWLKRSIDYKKNNNMETQLLFGIIQGGFYRELRKEAVERMLDMELPGFALGGISVGEPKDKMYEITDYTVSLLPEEKPRYLMGVGAPEDLVMGVSMGIDMFDCVLPTRLARHGVFYTKTGRRNIKNAQYKEDFSPLEEDCDCYTCRRFTKAYIRHLFLQHETFSYRLLTIHNLRFLFRLMEDVRRSIREGRLEEFKKEFLTQYLANDRENRLEKEEVWNRLLI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Dictyoglomus turgidum (strain Z-1310 / DSM 6724)
Length
388 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
45.138 kDa
Sequence
MIFEIIVRDKKTRARLGKLKTFHGEINTPVFMPVGTQGAVKTLSPEEVEKVGAEIILSNTYHLFLRPGHEIVRKGGGLHKFMGWEKPILTDSGGYQVFSLARLRRIDEDGIYFNSHIDGTRYFYTPELVMEIQKSLGSDIIMPLDICLGYGASYWETKEALEITLRWLKRSIDYKNNSNMDHQLLFGIVQGGFYKELRKEAVERMLNIDLPGLALGGISVGEPKDKMYEIIDYTVSLLPEEKPRYLMGVGAPEDLVVGVSMGIDMFDCVLPTRLARHGVFYTSKGRKNIKNAQYKEDFSPLEEDCDCYTCRKFTKAYIRHLFLQHETFSYRLLTIHNLRFLFRLMENIRKSIREGRLEEFKKEFLTEYLRDDRENRLEKEELWSKLLI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Campylobacter curvus (strain 525.92)
Length
388 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.682 kDa
Sequence
MKFEVLKTDGNARAGVLTTAHSVIQTPIFMPVGTVGAVKSLDATDMREILDAKIILANTYHMYLRPGSRVVAEFGGLHGFCKFNRSFLTDSGGFQAFSLRANTKNDEGGIKFKSHIDGSIHYFTPRSVLDTQYELDSDIMMILDDLVELPRDPHALGADEKARLKKRIDLSVTRTIKWAREAIDYHKFKQSQGAGLDQNIFGIIQGGTDYDARKICAQALCEMPFDGLAIGGLSVGEANEHMYETVEAVMPFIDAARPRYLMGVGTPEDIVENVQRGVDMFDCVMPTRNARNGTLFTSFGKIAIKNARFVNDHEPIDPECECYTCRRYSRGYLNHLFRAHELTFFRLASLHNLHYYLNLMKQIREAITAGKFSEFKREFYAKRSGGEI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Protochlamydia amoebophila (strain UWE25)
Length
387 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.405 kDa
Sequence
MFYSFCKVGQYMTYFKFELIHRSKKSRARVGRIHTPHGIIDTPNFVAVGTNGTVKALNNTMLHDIGLQLMFCNTYHMMLQPGTDIVRQAGGLHSFIQRKLPIITDSGGFQVFSLAYGSVADELKSRGTKKQGGCVLKITEEGVLFRSYRDGSKVLLTPESSIKAQKDLGADIIIPFDELPPYHIARDALKKSLDRTHRWEKRSLEAHLKNPQEQAMYAVVHGGIDPDLRKESCAILTELPFDGFAVGGSMGKTKDEMHTLLSLTLPLLPEDKPNHLLGIGDLPSIERSVPLGIDTFDSSYPTRAARHGILLTKQGPLNITKSEYATNFNSIEKGCLCPACHHFSLAYIHHLFKARELTCMSLATVHNLYFMVQLMEKYRKQIQEDLI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Polaromonas naphthalenivorans (strain CJ2)
Length
387 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.469 kDa
Sequence
MLEFEVLKTDPATVDSEGAYLGSYARRGQLTLNHGVVQTPIFMPVGTYGTVKGVTPQSLHDMNAQIILGNTFHLWMRPGLDVVAQFGGLHKFESWHKPILTDSGGFQVWSLGEMRKISEEGVKFASPVNGDKLFLTPEISMQIQTLLNSDIVMQFDECTPYDTKGHITTEGEARSSMELSRRWAKRCEIEFDKLENPNALFGIVQGGMFENLRQESLDALVEMDFPGYAVGGVSVGEPKEEMLRIMAHTPHRLPAHKPRYLMGVGTPEDLVEGVASGVDMFDCVMPTRNARNGHMFTRFGDLKIRNARYKSEEAPVDSTCGCYTCRNFSRAYMHHLDRCGEMLGPMLSSIHNLHYYLNLMQEVRGALDAGRFGEFVRQFKADRQRGV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)
Length
387 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.198 kDa
Sequence
MSTAFRWVEQARVGRARAGHLHTAHGVVPTPTFMPVGTVGTVKAMTMDSVRSTGAGIVLGNTYHLMLRPGAEKVRALGGLHRFMDWPGPILTDSGGFQVMSLGALRKLDQDGVTFNSHIDGSKHRLTPERSTDIQHALDATITMCFDECPALPAPPETIAQSMRLSMRWAARCREAFVPRAGYAQYGIIQGGTEPELRAESVRALTGIGFEGYAIGGLAVGEGQELMYATLDATVPLIPHDSPRYLMGVGTPDDLLGAVERGVDMFDCVMPTRAGRTARAYTERGTLNLRNARHADDTRPLSPHCDCLACTRHSRAYLHHLFRANEILGPMLLTWHNLAYYQRLMRGMRGAIVAGTLGAHAAGLRAEWAMEDWTPDEMPPPDLPPVP

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Length
386 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.843 kDa
Sequence
MVEATAQETDRPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGTAATVKALKPETVRATGADIILGNTYHLMLRPGAERIAKLGGLHSFMGWDRPILTDSGGYQVMSLSSLTKQSEEGVTFKSHLDGSRHMLSPERSIEIQHLLGSDIVMAFDECTPYPATPSRAASSMERSMRWAKRSRDAFDSRKEQAENAALFGIQQGSVFENLRQQSADALAEIGFDGYAVGGLAVGEGQDEMFRVLDFSVPMLPDDKPHYLMGVGKPDDIVGAVERGIDMFDCVLPTRSGRNGQAFTWDGPINIRNARFSEDLTPLDSECHCAVCQKWSRAYIHHLIRAGEILGAMLMTEHNIAFYQQLMQKIRDSISEGRFSQFAQDFRARYFARNS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Length
386 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.951 kDa
Sequence
MFFRLDLESCMKFEKLGQSGRARRGRLTLAHGVVETPVFMPVGTYGTVKGMLPRDIEEIQAQIILGNTFHLYLRPGLEVIKEHGGLHEFIKWDKPILTDSGGFQVFSLGAMRKIKEEGVTFRSPIDGSKVFLSPEISMEIQQVLNSDIVMIFDECTPYPATHEEAQKSLQLSLRWAKRCKTHHHEQLNNTNALFGIIQGGMYEDLRDESLNGLLEIGFDGYAIGGLSVGEPKEEMIKVLDYLPAKMPEDKPRYLMGVGKPEDIVEAVRRGVDMFDCVMPTRNARNGHYFVTDGLVRIRNSKYRHDQSPLDPHCDCYTCKNFTRAYLYHLEKCGEMLASMLGTIHNLRYYQRLTQGIRDALEQGTFDEFVTDFYTRRGLDVPPAPVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Pasteurella multocida (strain Pm70)
Length
385 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
44.013 kDa
Sequence
MKYELDKTDGNARRGRLVFERPQGTFTVETPAFMPVGTYGTVKGMTPEEVRATGAEILLGNTFHLWLRPGQEVMRKHGDLHDFMQWHRPILTDSGGFQVFSLGKLRKITEEGVKFQNPINGERIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKKSMEMSLRWAKRSRDRFDELGNKNALFGIIQGGVYEELRKVSVEGLVNIGFDGYAVGGLAVGEPKEDMHRILEYVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVSDGIVKIRNAKYREDTSPLDPECDCYTCKHYTKAYLYHLDKCGEILGARLNTIHNLRYYQRLMAQIRQAIEEDRFEAFVQEFYAKMGKPVPPMQSEIKSDEG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Haemophilus parasuis serovar 5 (strain SH0165)
Length
385 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
44.093 kDa
Sequence
MKYELKKTNGNARRGRLTFSRPKGEYHVETPAFMPVGTYGTVKGMTPEEVAQTGAQILLGNTFHLWLRPGQEIMRQHGDLHDFMQWHGPILTDSGGFQVFSLGKLRKIKEEGVYFQNPISGEKVFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKQSMEMSLRWAKRSRDRFDELQNPNALFGIIQGGVYEELRKVSVEKLVEIGFDGYAVGGLAVGEPKEDMHRILEYVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTNGIVKIRNAKYRNDISPLDPECDCYTCKNYTKAYLYHLDKCGEILGARLNTIHNLRYYQRLMAEIRQAIDEDRFDDFVVEFYQRIGKEVPPLQLAKEGENA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Length
385 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.925 kDa
Sequence
MDPFRFQVEARAGRARVGRLFTPHGAVETPLFMPVGTAGSVKGLMPKDLEAIGSQVLLANTYHLLLRPGPERVRALGGLHGFAGWKGPWLTDSGGFQVMSLGHMRRIDEEGVVFQSHLDGRLIKLTPERSIAVQEALGADLIMAFDECPPYPSPREYLEASLERTLRWLERSLKAKTRPDQALFGIAQGGTDPELRRRSTLETIRFDLPGYAIGGLAVGEPKEAMFAMVELSTRLLPEDRPRYLMGVGHPEDLVAAMGLGVDLFDCVYPTRTGRFGSALVPEGRLNLKNARFLEDRRPLEEGCDCYTCQTFGRAYLAHLVRAGEMLGGILLSLHNLRHLHRLTEAARQAIREGRYGDFAREFARRRFGREVPPWFREALAAGGHW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Length
385 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.826 kDa
Sequence
MDPFRFQVEARAGRARVGRLFTPHGAVETPLFMPVGTAGSVKGLMPKDLEAIGSQVLLTNTYHLLLRPGPERVRALGGLHGFAGWKGPWLTDSGGFQVMSLGHMRRIDEEGVVFQSHLDGRLIKLTPERSIAVQEALGADLIMAFDECPPYPSPREYLEASLERTLRWLERSLKAKTRPDQALFGIAQGGTDPELRRRSTLETIRFDLPGYAIGGLAVGEPKEAMFAMVELSTRLLPEDRPRYLMGVGHPEDLVAAMGLGVDLFDCVYPTRTGRFGSALVPEGRLNLKNARFLEDRRPLEEGCDCYTCQTFGRAYLAHLVRAGEMLGGILLSLHNLRHLHRLTEAARQAIREGRYGDFAREFARRRFGREVPPWFREALAAGGHG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Xylella fastidiosa (strain 9a5c)
Length
384 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.9 kDa
Sequence
MSRLQFQLQATDGAARRGQLSFPCGTVQTPAFMPVGTYGAVKGVLPGQLCDLGAEIILGNTFHLFLRPGLEVIADHGGLHGFMRWNGPILTDSGGFQVFSLAHRRKISEQGVTFAAPTDGAQVFLGPEESMKIQKVLNSDIVMIFDECTPYPATEDVARDSMELSLRWAQRSRDAHDALDNDAALFGIIQGGVHPDLRGRSLDGLQAIGFDGYGIGGLAVGESESERNVILEYLHPRVPADRPRYLMGVGRPEDLVESVARGVDMFDCVMPTRHARNGQYFTGFGTVKIRNACYARDVDPIEPGCGCPACVGGYTRAYLRHLDRCNEMLASMLGTLHNLWYYETLMANMRAAITAGTFFAFRRSFYLARGLDLPPLPEVAGCAG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Xylella fastidiosa (strain M12)
Length
384 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.967 kDa
Sequence
MSRLQFQLQATDGAARRGQLSFPCGTVQTPAFMPVGTYGAVKAVLPGQLCDLGAEIILGNTFHLFLRPGLEVIADHGGLHGFMRWNGPILTDSGGFQVFSLAHRRKISEQGVTFAAPTDGAQVFLGPEESMKIQKVLNSDVVMIFDECTPYPATEDVARDSMELSLRWAQRSRDAHDALDNDAALFGIIQGGVHPDLRGRSLDGLQAIGFDGYAIGGLAVGESESERNVILEYLHPRLPVDRPRYLMGVGRPEDLVESVARGVDMFDCVMPTRHARNGQYFTGFGTVKIRNACYARDVDPIEPGCGCPACVGGYTRAYLRHLDRCNEMLASMLGSLHNLWYYETLMANMRAAITAGTFFTFRHSFYLARGLDPPPLPEVASCAG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Desulfococcus oleovorans (strain DSM 6200 / Hxd3)
Length
384 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.483 kDa
Sequence
MFQFETTTACPDTKARTGKMTTAHGDVATPVFMPVGTLATVKSLSPEDLVACGAQIILGNTYHLYLRPGCDIIDAFSGVHAFMGWNRPLLTDSGGFQVFSLAKLSRITEEGAAFQSHLDGSSHLLTPESVIDIQNRLGSDIQMCLDQCIAFPAEKGAARDAANLTTRWAGRCRNRWQETGGPSRCGLFGIVQGGMFDDLRADSAGRLVDLDFSGYAVGGLSVGEPIETRLAVAEHTLSLLPPDRPRYIMGVGTPAELVELVALGADMFDCVMPTRNARNGKLFTSFGAINIRNACHAKETGPVDPACTCYTCTRFSRAYLRHLFMSRELLAYRLATLHNLFYYINLINDARAAVAAGRFAAFRKAFYAAQQATGPTGKEPCAGS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Synechococcus elongatus (strain PCC 7942)
Length
384 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.093 kDa
Sequence
MDRQCAVASLTAFQFQIDRQCSQTRGRACSFHTPHGIVETPRFMPVGTLATVKTVTPAQLRDTGAQMVLSNTYHLHLQPGEEIVAKAGGLHRFMNWSGPMLTDSGGFQVFSLSELRKIEERGVTFRSPRDGAVIEFTPERSIRIQNALGADVIMAFDECPPYPAERKDVEAAVARTYRWLERCINAHERPQDQALFGIVQGGVYLDLRQQAARDLVQLDLPGYAIGGVSVGEPSEEIHRIVEATAPLLPAHKPRYLMGVGTYREMVQAIAAGIDLFDCVIPTRLARHGAALVKGDRWNLKNAQFREDFQPLDEDCNCYCCQNFSRAYLNHLIRSREILGYTLLSIHNITELVRFTTRIREAILSDRFVEEFGHWLQPSAVPVSP

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Koribacter versatilis (strain Ellin345)
Length
384 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.854 kDa
Sequence
MSMSFSFQVEATQGAARAGRMITPHGEVETPVFMPVGTVATVKGIPQDLLEELGVQILLNNTYHLYLRPGVEQIRKLGGTHKFMSWDRSILTDSGGFQVFSLSELRKVTEEGVSFRSHLDGSSHLFSPESAMASQIGIGADIIMAFDECTEYPAERTRTERSMELTLRWAERSKNAFEAHKHEVPWFAERGKKSQALFGIVQGGMFPNLRKESAERTVEIGFPGYALGGFSVGEPREKTAELVANTVPLLPENKPRYLMGVGYPEEIVQYARMGIDMMDCVLPTRAARHGLLFTSEGRLTIKNQRFASDEGPLDPNCSCKVCKRYSRAYLRHLYASNEVLAQVLNTTHNLSYYLDTMRRVRQAIILGENSVSLPVVRSPHLSAT

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Ralstonia solanacearum (strain GMI1000)
Length
383 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.525 kDa
Sequence
MLNFDLLTTDGLARRGRMTLNHGVVETPIFMPVGTYGAVKAMSPVELKDIGAQIILGNTFHLWLRPALEVIDAHKGLHGFVGWDKPMLTDSGGFQVFSLGDLRKITEEGVHFASPINGDRLFLSPEISMQIQRRLNSDIVMQFDECTPYQIDGRPATEAEAAASMRMSLRWAQRSRNEFERERNPNALFGIVQGGMFEPLRDESLAGLQAIDADAGGQGFGGYAIGGLSVGEPKEDMIRVLQHVAPRLPANKPHYLMGVGTPEDLVAGVAAGIDMFDCVMPTRNARNGWLFTRFGDIKIKNAVHRNDPRPLDETCGCYTCRNFSRAYLHHLQRVGEILGARLNTIHNLHYYLELMADMRTAIESHSFAVFRARFAADRARGAL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
Length
383 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
44.349 kDa
Sequence
MRFKILQKDGLARTGIIETQRGIIHTPAFMPVGTNGTVKAMTPEEVRQIGYEIILSNTYHLYLRPGHETIKMIGGIHKFINWHCPILTDSGGFQIYSLASLRKITLEGVEFRSHIDGSLHFINPEKAIDIQLALGSDIMMVLDECIPYPADEEYVEKSIKLTTEWAKRCKEHFEKQDTYQALFGIIQGGVFSDLRIRALEELLKIDFHGYAIGGLSVGEPKTDMYKIVKDISPLMPEDKPHYLMGVGDLIDVLHAVEHGIDMFDCVIPTRNARNGTLFTSQGRISIKRSEFKEDLSPLDPDCDCYTCKNYSRAFLRHLYTCREILSMRLNTIHNLYFYCRFFEKMRQAIAERRFQEFKKEWLPVLEKNFYQESNDFHHSLENY

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Psychrobacter arcticus (strain DSM 17307 / 273-4)
Length
383 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.068 kDa
Sequence
MQFVLHKTASGVTRARRGTVHLNHGDVQTPAFMPVGTYGTVKGMLPRDIEAIGADIILGNTFHLWLRPGTDIIDKFGGLHKFMHWDKPILTDSGGFQVFSLGAMRKITEEGVTFKSPIDGAKVFLSPEKSMQIQYSLNSDIVMQFDECTPYPATHDEAKKSLELSLRWGQRCVDEHKKLGSTNALFGIIQGSMYADLRKQSLEGLLEIGFDGYAIGGLSVGEPKEEMIDVLDYIANDMPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHYFVTGDVDNAGVVRIRNSQYRTDEGPLDPECDCYTCQNFSRAYLSHLNKCKEMLGAQLATIHNLRYYQRLMQGIRDAIEQDKFDEFVTEFYSKRGQTVPELNLR

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Psychrobacter cryohalolentis (strain K5)
Length
383 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.097 kDa
Sequence
MQFVLHKTASGVTRARRGTVHLNHGDVQTPAFMPVGTYGTVKGMLPRDIEAIGADIILGNTFHLWLRPGTDIIDKFGGLHKFMHWDKPILTDSGGFQVFSLGAMRKITEEGVTFKSPIDGAKVFLSPEKSMQIQYSLNSDIVMQFDECTPYPATHDEAKKSLELSLRWGQRCVDEHKNLGSTNALFGIIQGSMYADLRKQSLEGLLEIGFDGYAIGGLSVGEPKEEMIDVLDYIADDMPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHYFVTGDADNAGVVRIRNSQYRTDEGPLDPECDCYTCQNFSRAYLSHLNKCKEMLGAQLATIHNLRYYQRLMQNIRDAIEQDKFDEFVNEFYSKRGQTVPELNLR

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Psychrobacter sp. (strain PRwf-1)
Length
383 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.446 kDa
Sequence
MQFTLHKTAAGESRARRGTVTVNHGEIRTPAFMPVGTYGTVKGMLPRDIEDIGADIILGNTFHLWLRPGTEVIDKFGGLHQFMNWNKPILTDSGGFQVFSLGAMRKITEEGVAFKSPIDGAKVFLSPEKSMQIQYSLNSDIVMQFDECTPYPATYSEAQKSLELSLRWGQRCVDEHKKLGNTNALFGIVQGSMYEDLRRQSMDGLLEIGFDGYAIGGLSVGEPKEEMISVLNYMPELMPADKPRYLMGVGKPEDILEAVRRGVDMFDCVMPTRNARNGHYFVTGNEDNQGIVRIRNSQYREDQGPLDPECDCYCCQNFSRAYLYHLNKCKEMLGAQLATIHNLRYYQRLMQGIRDAIDEDRFDEFVADFYHRRGQDVPPLELK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Ralstonia pickettii (strain 12J)
Length
383 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.357 kDa
Sequence
MLKYELLTTDGLARRGRMTLNHGVVETPIFMPVGTYGAVKAMSPAELKDIGAQIILGNTFHLWLRPGLEVMDAHKGLHGFNGWDKPILTDSGGFQVFSLGDLRKITEDGVTFASPINGDKLFLSPEISMQIQRRLNSDIVMQFDECTPYKIGDRPATEAEAAASMRMSLRWAQRSRNEFEREKNPNALFAIVQGGMFENLRDESLAGLQAIDADAGGEGFGGYAIGGLSVGEPKEDMMRVLQHVAPRLPADKPHYLMGVGTPEDLVAGVAAGVDMFDCVMPTRNARNGWLFTRFGDIKIKNAVHRNDPRPLDETCGCYTCSNFSRAYLHHLQRVGEILGARLNTIHNLYYYLELMAEMRTAIESHGFAAFQARFAADRARGAL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus clausii (strain KSM-K16)
Length
383 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.432 kDa
Sequence
MTAAITYEHIKTCKQSGARLGRVHTPHGTIETPMFMPVGTLATVKTMSPEDLKAMDAQIILSNTYHLWLRPGEEIIKEAGGLHQFMNWDKPILTDSGGFQVFSLSDLRKITEEGVHFRNHLSGEKLFLSPEKAMQIQHVLGSDIMMAFDECPPYPADHSYMKASVERTSRWAERCLAEHKRSGKDSVQGLFGIIQGGEYEDLRKQSANDLTALDFPGYAVGGLSVGEPKDVMNHVLEFTTPLMPEDKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSAGRLVVRNAKYARDFSPLDEKCDCHVCRTYSRAYIRHLIKCEETFGFRLTTYHNLYFLLNLMKQVRQAIMDDCLLDFREQFFEEYGFNKENARNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Actinobacillus pleuropneumoniae serotype 5b (strain L20)
Length
382 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.359 kDa
Sequence
MKYELKTTSGNARRGRLTFSRPKGEYVVETPAFMPVGTYGTVKGMTPEEVAATGAQILLGNTFHLWLRPGQEVMKSHGDLHGFMQWHGPILTDSGGFQVFSLGKLRKIKEEGVTFQNPISGEKIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKNSMEMSLRWAKRSRDRFDELQNPRALFGIVQGGTYEELRKISVEGLVNIGFDGYAVGGLAVGEPKEEMHRILEFTTPLLPQDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVSNGIVKIRNAKYKTDTTPLDPECDCYTCKNYTKAYLYHLDKCGEILGARLNTIHNLRYYQRLMAQIRQAIEEDRFDDFVVEFYAKIGKEVPPLQSEVNK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Actinobacillus pleuropneumoniae serotype 7 (strain AP76)
Length
382 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.359 kDa
Sequence
MKYELKTTSGNARRGRLTFSRPKGEYVVETPAFMPVGTYGTVKGMTPEEVAATGAQILLGNTFHLWLRPGQEVMKSHGDLHGFMQWHGPILTDSGGFQVFSLGKLRKIKEEGVTFQNPISGEKIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKNSMEMSLRWAKRSRDRFDELQNPRALFGIVQGGTYEELRKISVEGLVNIGFDGYAVGGLAVGEPKEEMHRILEFTTPLLPQDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVSNGIVKIRNAKYKTDTTPLDPECDCYTCKNYTKAYLYHLDKCGEILGARLNTIHNLRYYQRLMAQIRQAIEEDRFDDFVVEFYAKIGKEVPPLQSEVNK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Actinobacillus pleuropneumoniae serotype 3 (strain JL03)
Length
382 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.332 kDa
Sequence
MKYELKTTSGNARRGRLTFSRPKGEYVVETPAFMPVGTYGTVKGMTPEEVAATGAQILLGNTFHLWLRPGQEVMKSHGDLHGFMQWHGPILTDSGGFQVFSLGKLRKIKEEGVTFQNPISGEKIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKNSMEMSLRWAKRSRDRFDELQNPRALFGIVQGGTYEELRKISAEGLVDIGFDGYAVGGLAVGEPKEEMHRILEFTTPLLPQDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVSNGIVKIRNAKYKTDTTPLDPECDCYTCKNYTKAYLYHLDKCGEILGARLNTIHNLRYYQRLMAQIRQAIEEDRFDDFVVEFYAKIGKEVPPLQSEVNK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
Length
382 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.489 kDa
Sequence
MMKYELKSTSGMARRGRLTFSRPQGECYVETPAFMPVGTYGTVKGMTPEEVKATGAQILLGNTFHLWLRPGQEIMKMHGDLHDFMQWHGPILTDSGGFQVLSLGKLRKIKEEGVTFQNPISGEKIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATLEYAKKSMEMSLRWAKRSRTRFDELANPRALFGIVQGSTYEELRRESVKGLINIGFDGYAVGGLAVGEPKEEMHRILEFTTPLLPQDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVSDGVVKIRNAKYKNDTTPLDAECDCYTCKNYTKAYLYHLDKCGEILGARLNTIHNLRYYQRLMAQIRQAIEQDCFDEFVVEFYAKIGKEVPPLHLKSE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Haemophilus influenzae (strain 86-028NP)
Length
382 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.608 kDa
Sequence
MKYELDKTSGNARRGRLVFERPQGTFSVETPAFMPVGTYGTVKGMTPEEVRATGAEILLGNTFHLWLRPGQEIMRKHGDLHDFMQWHRPILTDSGGFQVFSLGKLRKITEEGVKFQNPINGERIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKKSMEMSLRWAKRSHDRFDELGNKNALFGIIQGGVFEELRKVSLEGLVNIGFDGYAVGGLAVGEPKEDMHRILEYICPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGIVKIRNAKYRDDTSPLDPECDCYTCKNYTKAYLYHLDKCGEILGARLNTIHNLRYYQRLMAEIRQAIEDDRFDDFVVEFYARMGKPVPPLQLADNS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Haemophilus influenzae (strain PittEE)
Length
382 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.641 kDa
Sequence
MKYELDKTSGNARRGRLVFERPQGTFSVETPAFMPVGTYGTVKGMTPEEVRATGAEILLGNTFHLWLRPGQEIMRKHGDLHDFMQWHRPILTDSGGFQVFSLGKLRKITEEGVKFQNPINGERIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKKSMEMSLRWAKRSRDRFDELGNKNALFGIIQGGVFEELRKVSLEGLVNIGFDGYAVGGLAVGEPKEDMHRILEYICPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGIVKIRNAKYRDDTSPLDPECDCYTCKNYTKAYLYHLDKCGEILGARLNTIHNLRYYQRLMAEIRQAIEDDRFDDFVVEFYARMGKPVPPLQLADKS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Haemophilus influenzae (strain PittGG)
Length
382 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.597 kDa
Sequence
MKYELDKTSGNARRGRLVFERPQGTFSVETPAFMPVGTYGTVKGMTPEEVRATGAEILLGNTFHLWLRPGQEIMRKHGDLHDFMQWHRPILTDSGGFQVFSLGKLRKITEEGVKFQNPINGERIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKKSMEMSLRWAKRSRARFDELGNKNALFGIIQGGVFEELRKVSLEGLVNIGFDGYAVGGLAVGEPKEDMHRILEYICPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGIVKIRNAKYRDDTSPLDPECDCYTCKNYTKAYLYHLDKCGEILGARLNTIHNLRYYQRLMAEIRQAIEDDRFDDFVVEFYARMGKPVPPLQLADKS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
382 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.627 kDa
Sequence
MKYELDKTSGNARRGRLVFERPQGTFSVETPAFMPVGTYGTVKGMTPEEVRATGAEILLGNTFHLWLRPGQEVMRKHGDLHDFMQWHRPILTDSGGFQVFSLGKLRKITEEGVKFQNPINGERIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKKSMEMSLRWAKRSRDRFDELGNKNALFGIIQGGVFEELRKVSLEGLVNIGFDGYAVGGLAVGEPKEDMHRILEYICPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGIVKIRNAKYRDDTSPLDPECDCYTCKNYTKAYLYHLDKCGEILGARLNTIHNLRYYQRLMAEIRQAIEDDRFDDFVVEFYARMGKPVPPLQLADKS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Sodalis glossinidius (strain morsitans)
Length
382 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.335 kDa
Sequence
MEYQLLKTDGQARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQAVMKLHGDLHDFMQWHGPILTDSGGFQVFSLGDIRKITEEGVYFRNPINGDTIFLSPEKSMEIQYDLGSDIVMIFDECTSYPSDWDYAKQSMEMSLRWAARSRQRFDELGNHNALFGIIQGSVYEDLRDVSVKRLVEIGFDGYAVGGLAVGEPKADMHRILAHLCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNARYKDDVAPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIDEGKLEHFVGEFYRRTGKPAPPLVVELHNNEGI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Lactococcus lactis subsp. lactis (strain IL1403)
Length
382 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.342 kDa
Sequence
MTEHAIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTMSPEELKTLGSGIILSNTYHLWLRPGDELVAEAGGLHKFMNWDQPILTDSGGFQVYSLVQNKKNITEEGVKFKSHLDGRELFLNPEKAISIQNNLGSDIMMSFDECPPFYQPYDYVKASVERTSRWAERGLNAHRRPNDQGLFGIVQGAGFEDLRRQSARDLTSMDFAGYSIGGLAVGESHKEMNAVLDFTTPMLPEDKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTLMTHFGRVNIRNAKYEHDFTPLDPMCDCYTCTNYTRAYLRHLIKADETFGLRLCSYHNLHFLVNLMKDVRGAIMDDNLLEFREDFCERYGYNQPNAKDF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
Length
382 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.37 kDa
Sequence
MTEHAIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTMSPEELKTLGSGIILSNTYHLWLRPGDELVAEAGGLHKFMNWDQPILTDSGGFQVYSLVQNKKNITEEGVKFKSHLDGRELFLNPEKAISIQNNLGSDIMMSFDECPPFYQPYDYVKASVERTSRWAERGLNAHRRPNDQGLFGIVQGAGFEDLRRQSASDLTSMDFAGYSIGGLAVGESHKEMNAVLDFTTPMLPEDKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTLMTHFGRVNIRNAKYEYDFTPLDPMCDCYTCTNYTRAYLRHLIKADETFGLRLCSYHNLHFLVNLMKDVRQAIMDDNLLEFREDFCERYGYNQPNAKDF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Lactococcus lactis subsp. cremoris (strain SK11)
Length
382 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.344 kDa
Sequence
MTEHAIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTMSPEELKTLGSGIILSNTYHLWLRPGDELVAEAGGLHKFMNWDQPILTDSGGFQVYSLVQNKKNITEEGVKFKSHLDGRELFLNPEKAISIQNNLGSDIMMSFDECPPFYQPYDYVKASVERTSRWAERGLNAHRRPNDQGLFGIVQGAGFEDLRRQSASDLTSMDFAGYSIGGLAVGESHKEMNAVLDFTTPMLPEDKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTLMTHFGRVNIRNAKYEHDFTPLDPMCDCYTCTNYTRAYLRHLIKADETFGLRLCSYHNLHFLVNLMKDVRQAIMDDNLLEFREDFCERYGYNQPNAKDF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.365 kDa
Sequence
MKYELQTTDGRARRGRLIFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMNWHGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDSIFLSPEKSMEIQNDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRQRFDELENKNALFGIIQGSVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDVSSLDEHCDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLELFVVDFYQRIGKPIPPLAEKDVAASN

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.419 kDa
Sequence
MKYELQTTDGRARRGRLIFERGVVETPAFMPVGTYGTVKGMTPEEVKDTGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWHGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDSIFLSPEKSMEIQHDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRQRFDELENKNALFGIIQGSVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKDDVSPLDEHCDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLEHFVVDFYQRIGKPIPPLAEKDVAAGN

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Xanthomonas axonopodis pv. citri (strain 306)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.126 kDa
Sequence
MSRLQFQLQATDGHARRGRLTFPRGTVETPAFMPVGTYGSVKGILPEQIRALGAEIILGNTFHLYLRPGLEVIGDHGGLHGFARWDGPILTDSGGFQVFSLAHRRKITEQGVTFSSPTDGARVFLGPEESMKIQKVLDSDIVMIFDECTPYPATEDVARRSMELSLRWAQRSRDAHDGLGNDAALFGIVQGGVHPDLRSRSLDGLQAIGFDGYAIGGLAVGEPEHERNAMLEHLHPRLPAERPRYLMGVGRPEDLVEGVARGVDMFDCVMPTRNARNGHYFTSFGTVRIRNAKYERDLDTIEPGCGCHACSSGYTRAYLRHLDRCNEMLAPMLGTLHNLWYYEKLMADMRAAIASGTFVEFRRSFYAARGATTPPLPGETS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Xanthomonas campestris pv. vesicatoria (strain 85-10)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.029 kDa
Sequence
MSRLQFQLQATDGHARRGRLTFPRGTVETPAFMPVGTYGSVKGILPEQIRALGAEIILGNTFHLYLRPGLEVIGDHGGLHGFARWDGPILTDSGGFQVFSLAHRRKITEQGVTFSSPTDGARVFLGPEESMKIQKVLDSDIVMIFDECTPYPATEDVARRSMELSLRWAQRSRDAHDGLGNDAALFGIVQGGVHPDLRSRSLDGLQGIGFDGYAIGGLAVGEPEHERNAMLEHLHPRLPAERPRYLMGVGRPEDLVEGVARGVDMFDCVMPTRNARNGHYFTSFGTVRIRNAKYERDLDTIEPGCGCHACSSGYTRAYLRHLDRCNEMLAPMLGTLHNLCYYEKLMADMRAAIASGTFVEFRRSFYAARGATTPPLPGETS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Xanthomonas campestris pv. campestris (strain 8004)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.138 kDa
Sequence
MSRLQFQLQTTDGHARRGRLTFPRGTVETPAFMPVGTYGSVKGILPEQIRALGAEIILGNTFHLYLRPGLDVIGDHGGLHGFARWDGPILTDSGGFQVFSLAHRRKITEQGVTFSSPNDGARVFLGPEESMQIQKVLDSDIVMIFDECTPYPATEDVARRSMELSLRWAQRSRQAHDGLGNDAALFGIVQGGVHPDLRSRSLDGLQAIGFDGYAIGGLAVGEPEHERNAMLEHLHPRLPAERPRYLMGVGRPEDLVEGVARGVDMFDCVMPTRNARNGHYFTSFGTVRIRNAKYERDLDTIEPGCGCHACSSGYTRAYLRHLDRCNEMLAPMLGTLHNLWYYEKLMADMRAAIAAGTFVEFRRSFYAARGATTPPLPGESS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Xanthomonas campestris pv. campestris (strain B100)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.125 kDa
Sequence
MSRLQFQLQTTDGHARRGRLTFPRGTVETPAFMPVGTYGSVKGILPEQIRALGAEIILGNTFHLYLRPGLDVIGDHGGLHGFARWDGPILTDSGGFQVFSLAHRRKITEQGVTFSSPTDGARVFLGPEESMQIQKVLDSDIVMIFDECTPYPATEDVARRSMELSLRWAQRSRQAHDGLGNDAALFGIVQGGVHPDLRSRSLDGLQAIGFDGYAIGGLAVGEPEHERNAMLEHLHPRLPAERPRYLMGVGRPEDLVEGVARGVDMFDCVMPTRNARNGHYFTSFGTVRIRNAKYERDLDTIEPGCGCHACSSGYTRAYLRHLDRCNEMLAPMLGTLHNLWYYEKLMADMRAAIAAGTFVEFRRSFYAARGATTPPLPGESS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.138 kDa
Sequence
MSRLQFQLQTTDGHARRGRLTFPRGTVETPAFMPVGTYGSVKGILPEQIRALGAEIILGNTFHLYLRPGLDVIGDHGGLHGFARWDGPILTDSGGFQVFSLAHRRKITEQGVTFSSPNDGARVFLGPEESMQIQKVLDSDIVMIFDECTPYPATEDVARRSMELSLRWAQRSRQAHDGLGNDAALFGIVQGGVHPDLRSRSLDGLQAIGFDGYAIGGLAVGEPEHERNAMLEHLHPRLPAERPRYLMGVGRPEDLVEGVARGVDMFDCVMPTRNARNGHYFTSFGTVRIRNAKYERDLDTIEPGCGCHACSSGYTRAYLRHLDRCNEMLAPMLGTLHNLWYYEKLMADMRAAIAAGTFVEFRRSFYAARGATTPPLPGESS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Xanthomonas oryzae pv. oryzae (strain MAFF 311018)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.114 kDa
Sequence
MSRLQFQLQATDGHARRGRLTFPRGTVETPAFMPVGTYGSVKGILPEHIRALGAEIILGNTFHLYLRPGLDVIGDHGGLHGFARWDGPILTDSGGFQVFSLAHRRKITEQGVTFSSPTDGARVFLGPEESMKIQKVLDSDIVMIFDECTPYPATEDLARRSMELSLRWAQRSRDAHDGLGNDAALFGIVQGGVHPDLRSRSLDGLQSIGFDGYAIGGLAVGEPEHERNAMLEHLHPRLPAECPRYLMGVGRPEDLVEGVARGVDMFDCVMPTRNARNGHYFTSFGTVRIRNAKYERDLDTIEPGCGCHACSSGYTRSYLRHLDRCNEMLAPMLGTLHNLWYYEKLMADMRAAIASGTFVEFRRSFYAARGATTPPLPGETS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Xanthomonas oryzae pv. oryzae (strain PXO99A)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.114 kDa
Sequence
MSRLQFQLQATDGHARRGRLTFPRGTVETPAFMPVGTYGSVKGILPEHIRALGAEIILGNTFHLYLRPGLDVIGDHGGLHGFARWDGPILTDSGGFQVFSLAHRRKITEQGVTFSSPTDGARVFLGPEESMKIQKVLDSDIVMIFDECTPYPATEDLARRSMELSLRWAQRSRDAHDGLGNDAALFGIVQGGVHPDLRSRSLDGLQSIGFDGYAIGGLAVGEPEHERNAMLEHLHPRLPAECPRYLMGVGRPEDLVEGVARGVDMFDCVMPTRNARNGHYFTSFGTVRIRNAKYERDLDTIEPGCGCHACSSGYTRSYLRHLDRCNEMLAPMLGTLHNLWYYEKLMADMRAAIASGTFVEFRRSFYAARGATTPPLPGETS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.114 kDa
Sequence
MSRLQFQLQATDGHARRGRLTFPRGTVETPAFMPVGTYGSVKGILPEHIRALGAEIILGNTFHLYLRPGLDVIGDHGGLHGFARWDGPILTDSGGFQVFSLAHRRKITEQGVTFSSPTDGARVFLGPEESMKIQKVLDSDIVMIFDECTPYPATEDLARRSMELSLRWAQRSRDAHDGLGNDAALFGIVQGGVHPDLRSRSLDGLQSIGFDGYAIGGLAVGEPEHERNAMLEHLHPRLPAECPRYLMGVGRPEDLVEGVARGVDMFDCVMPTRNARNGHYFTSFGTVRIRNAKYERDLDTIEPGCGCHACSSGYTRSYLRHLDRCNEMLAPMLGTLHNLWYYEKLMADMRAAIASGTFVEFRRSFYAARGATTPPLPGETS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Helicobacter hepaticus (strain ATCC 51449 / 3B1)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.842 kDa
Sequence
MQVTLQAQDGGARALSLKLAHSEVQTPVFMPVGTQGCVKALDSRDMSEILNAQIILVNTYHMYLRIGIERLKNFGGIARFAHFDRSYLSDSGGFQAFSLNKNAKVTNEGVAFKSHIDGSKHFFSPEYVLDIQYALNSDIMMVLDDLVGLPSSEERIADSIARTSDWAQKSLIYHQSQKARGLGLNNNLFAIIQGGVNEHFRTLCAKQLVDMGDFDGFAIGGLAVGETSEQMYKTISFTTPLMPVNKPRYLMGVGTPENIIESIALGVDMFDCVMPTRNARNATLFTHFGKINIKAAIFSNDQSPIDELCDCYTCQHFTRAYLCHLFRSQEMTYYRLASLHNLHYYLNLMREAREAILQGTFSAYRSSFYALREMEIPNNEY

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.407 kDa
Sequence
MTEPAIRYRLIKKDKHTGARLGELITPHGTFPTPMFMPVGTLATVKTMSPEELKEMGAGVILSNTYHLWLRPGEDLVEEAGGLHKFMNWDQPILTDSGGFQVFSLSDMRKIEEEGVHFRNHLNGSKMFLSPEKAINIQNKLGSDIMMSFDECPPFDESYEYVKRSIERTSRWAERGLKAHANPDRQGLFGIVQGAGFEDLRRQSAKDLVSMDFPGYSIGGLSVGESKEEMNRVLDFTTPLIPENKPRYLMGVGAPDSLIDGVIRGIDMFDCVLPTRIARNGTCMTSQGRLVVKNAQYARDFRPLDEKCDCYVCRNYTRAYIRHLIKCDETFGIRLTSYHNLYFLLDLMKNVRQAIMDDNLLEFRQAFFEEYGFNKANAKSF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.297 kDa
Sequence
MNDSLQAIPNQPFSFFTQASCSHTQARAGQFFTPHGVVETPRFMPVGTLANIKTVTPEQLRGTGAQMILANTYHLHLQPGEGIVAAAGGLHRFMGWTGPILTDSGGFQVFSLSELRSIAEAGVTFRSPRDGEEIYLSPEKAIAIQNQLGADVIMAFDECAPYPADRSTVTEAVERTTRWLERCCKAHDRVEDQALFGIIQGGTYGDLRQQSARSLVEFDLPGYAIGGVSVGEPPELIEKIVKFTTPLLPEHKPRYLMGVGTYREMVQAIAAGIDLFDCVIPTRLARHGNALVRGERWNLKNSRFREDFQPLDQSCACYTCQNFSRAYLSHLLRARELLAYTLLSIHNITELISFTQKIRQAILHDRFSSEFASWLTSPSPS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Lysinibacillus sphaericus (strain C3-41)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.37 kDa
Sequence
MTQPAIRYELLHTCKQTGARLGIVHTPHGSFETPAFMPVGTQATVKTMSPEELKEMNAGIILSNTYHLWLRPGNDIVKEAGGLHKFMNWDRPILTDSGGFQVFSLSQFRKIEEEGVHFRNHLNGDKLFLSPEKAMEIQNDLGSDIMMAFDECPPYPATHEYMLQSVDRTTRWAKRCKEAHSRPEEQGLFGIIQGGEYEDLRRRSAEALVELDFPGYAIGGLSVGEPKDIMNRVLEFTTPLMPANKPRYLMGVGSPDSLIDGAIRGVDMFDCVLPTRIARNGTLMTSEGRLVVKNAKYARDFGPIDPNCDCYTCKNYSRAYIRHLIRTEETFGIRLTSYHNLHFLLKLMEQVREAIRQDRLGDFREEFFEKYGFNGPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.615 kDa
Sequence
MSQQPIRYEFIKACKQTGARLGRVHTPHGSFETPVFMPVGTLATVKTMSPEELKEMGADIILSNTYHLWLRPGHDIVKEAGGLHQFMNWNRAILTDSGGFQVFSLSEFRKIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPYPAEYDYMKKSVERTSRWAERCLKAHNRPDEQGLFGIVQGGEYENLRKQSAKDLISLDFPGYAIGGLSVGEPKDVMNRVLEFTTPLLPADKPRYLMGVGSPDSLIDGAIRGVDMFDCVLPTRIARNGTLMTSEGRLVVKNAKYERDFRPIDEQCDCYTCRNYSRAYIRHLIRCNETFGIRLTSYHNLYFLLKLMGQVRDAIREDRLGDFREEFFERYGFNKPNAKSF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus pumilus (strain SAFR-032)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.575 kDa
Sequence
MSQLPIRYEFIKSCKQTGARLGRVHTPHGSFDTPVFMPVGTLATVKTMAPEELKAMEAGIILSNTYHLWLRPGHDIVKEAGGLHKFMNWDRAILTDSGGFQVFSLSEFRKIEEEGVHFRNHLNGDKLFLSPEKAMDIQNALGSDIMMAFDECPPYPAEYDYMKRSVERTSRWAERCLTAHQRPEDQGLFGIIQGGEYEELRKQSAKDLVSLDFPGYAIGGLSVGEPKDVMNRVLEFTTPLLPADKPRYLMGVGSPDSLIDGAIRGVDMFDCVLPTRIARNGTLMTSEGRLVVKNAKYERDFRPIDENCDCYTCKNYTRAYIRHLIKTNETFGIRLTTYHNLHFLLKLMEQVREAIREDRLGDFKEEFFERYGFNEPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus subtilis (strain 168)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.711 kDa
Sequence
MAEQPIRYEFIKECKQTGARLGKVHTPHGSFETPVFMPVGTLATVKTMSPEELKAMDAGIILSNTYHLWLRPGQDIVKEAGGLHKFMNWDRAILTDSGGFQVFSLSKFRNIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPYPAEYDYMKRSVERTSRWAERCLNAHNRQDEQGLFGIVQGGEYEDLRTQSAKDLISLDFPGYAIGGLSVGEPKDVMNRVLEFTTPLLPKDKPRYLMGVGSPDALIDGAIRGVDMFDCVLPTRIARNGTVFTAEGRLNMKNAKFERDFRPIDEECDCYTCKNYTRAYIRHLIRCNETFGLRLTTYHNLHFLLHLMEQVRQAIREDRLGDFREEFFERYGYNKPNAKSF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42)
Length
381 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.666 kDa
Sequence
MAEQPIRYEFIKECKQTGARLGRVHTPHGSFETPVFMPVGTLATVKTMSPDELKSMDAGIILSNTYHLWLRPGHDIVKEAGGLHKFMNWDRAILTDSGGFQVFSLSKFRNIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPYPAEYDYMKRSVERTSRWAERCLEAHGRSDEQGLFGIVQGGEYEDLRTQSAKDLVSLDFPGYAIGGLSVGEPKHVMNRVLEFTTPLLPKDKPRYLMGVGSPDALIDGAIRGVDMFDCVLPTRIARNGTVFTNEGRLNMKNAKYERDFRPIDEECSCHTCKNYSRAYIRHLIRCNETFGIRLTTYHNLHFLLHLMEQVRQAIREDRLGDFREEFFERYGYNKPNAKSF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.206 kDa
Sequence
MEPAIKYRLIKTDKHTGARLGEIITPHGTFPTPIFMPVGTQATVKAMSPEELEDLGADIILSNTYHLWVRPGEDIVKEGGGLHQFMNWKKGILTDSGGFQVFSLAKLRDITEEGVHFKNELNGANMFLSPEKAIQIENDLGPDIMMSFDECPPYFESYDYVKHSVERTSRWAERGLKAHRNPETQGLFGIIQGAGFEDLRRQSAKDLVSMDFPGYSIGGLSVGESKEEMNRVLDFTTQLIPENKPRYLMGVGSPDALIDGVLRGVDMFDCVLPTRIARNGTCMTSHGRLVVKNAKYARDFTPIDDNCQCYTCRNYTRAYIRHLIKTDETFGLRLTSIHNVYFLVHLMKDVRQAIMDDNLLEFRQNFFEEYGYNKENSKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Geobacillus kaustophilus (strain HTA426)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.27 kDa
Sequence
MTTPIRFELIKTCRQTGARLGILHTPHGSFETPMFMPVGTLATVKTLSPEELKEMGAGVILSNTYHLWLRPGHDIVEEAGGLHAFMNWDRGILTDSGGFQVFSLSEFRRIEEEGVYFRNHLNGDKLFLSPEKAVEIQNALGADIIMAFDECPPYPATYEYMKQSIERTSRWAERCLKAHRRPNEQGLFGIVQGGEYEELRRQSARDLVSLDFPGYAVGGLSVGEPKEVMNRVLEFTTPLLPADKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIGRNGTVMTSEGRVVIKNAQYARDFSPLDPNCDCYTCRNYTRAYIRHLIKCDETFGIRLTSYHNVYFLIKLMEQVRQAIREDRLADFREEFFECYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Geobacillus thermodenitrificans (strain NG80-2)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.273 kDa
Sequence
MTTPIRFELIKTCRQTGARLGILHTPHGSFETPMFMPVGTLATVKTLSPEELKEMGAGVILSNTYHLWLRPGHDIVAEAGGLHAFMNWDRGILTDSGGFQVFSLSEFRRIEEEGVYFRNHLNGDKLFLSPEKATEIQNALGADIIMAFDECPPYPATYDYMKRSVERTSRWAERCLKAHRRSNEQGLFGIVQGGEYEDLRRQSARDLVSLDFPGYAVGGLSVGEPKDVMNRVLEFTTPLLPTDKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIGRNGTVMTSEGRVVIKNAQYARDFTPLDPNCDCYTCRNYTRAYIRHLIKCDETFGIRLTSYHNVYFLIKLMEQVRQAIREDRLADFREEFFERYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus carnosus (strain TM300)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.418 kDa
Sequence
MKPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELHDINAKIILGNTYHLWLQPGNELIKRAGGLHQFMNWDGPILTDSGGFQVFSLSNLRKITEEGVYFRHHKNGSKLFLSPEKSMEIQNDLGSDIMMAFDECPPMPAEYKYVKDSIERTTRWAERCLKAHARPEDQALFGIIQGGEYKDLRQQSAEELVKLDFPGYAIGGLSVGEPKPVMYDMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSEGRVVIKNAKYADDLGPLDPNCDCYTCRNYSRAYLRHLIKAEETFGIRLTTYHNLYFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC SS700)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.114 kDa
Sequence
MTDHPIKYRLIKQEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIAKAGGLHKFMNWDQAILTDSGGFQVYSLADSRNITEEGVTFKNHLNGAKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLNAHRRPHDQGLFGIVQGAGFEDLRRQSARDLVSMDFPGYSIGGLAVGETHDEMNAVLDFTVPMLPNDKPRYLMGVGAPDSLIDAVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAKFAEDFTPLDPNCDCYTCKNYTRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKDVRQAIMDDNLLEFRQDFMERYGYGMNNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus agalactiae serotype III (strain NEM316)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.114 kDa
Sequence
MTDHPIKYRLIKQEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIAKAGGLHKFMNWDQAILTDSGGFQVYSLADSRNITEEGVTFKNHLNGAKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLNAHRRPHDQGLFGIVQGAGFEDLRRQSARDLVSMDFPGYSIGGLAVGETHDEMNAVLDFTVPMLPNDKPRYLMGVGAPDSLIDAVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAKFAEDFTPLDPNCDCYTCKNYTRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKDVRQAIMDDNLLEFRQDFMERYGYGMNNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.114 kDa
Sequence
MTDHPIKYRLIKQEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIAKAGGLHKFMNWDQAILTDSGGFQVYSLADSRNITEEGVTFKNHLNGAKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLNAHRRPHDQGLFGIVQGAGFEDLRRQSARDLVSMDFPGYSIGGLAVGETHDEMNAVLDFTVPMLPNDKPRYLMGVGAPDSLIDAVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAKFAEDFTPLDPNCDCYTCKNYTRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKDVRQAIMDDNLLEFRQDFMERYGYGMNNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus equi subsp. equi (strain 4047)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.034 kDa
Sequence
MTNYPITYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEIGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQAILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVSMDFPGYSIGGLAVGESHAEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFAEDFTPLDHHCDCYTCQHYTRAYLRHLLKADETFGMRLTSYHNLYFLVNLMKQVRQAILDDNLLEFRQDFLERYGYNSSSRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.145 kDa
Sequence
MSDSPIQYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKQMGSGIILANTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHSRPHDQGLFGIVQGAGFEDLRRQSAQDLVSMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVVKNAQFEEDFTPLDHNCDCYTCTNYTRAYIRHLLKADETFGLRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFREDFMERYGYNRSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.218 kDa
Sequence
MTHSPIQYRLIKKEKHTGARLGEIITPHGVFPTPMFMPVGTQATVKTQSPEELKEMKAGIILANTYHLWLRPGDDLVARAGGLHKFMNWDQPILTDSGGFQVYSLAEKRNITEEGVTFKNHLNGARMFLTPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKASIERTSRWAERGLKAHRRPQDQGLFGIVQGAGFEDLRRQSTADLVSMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSRGRLVVKNAQYAEDFTPLDHDCDCYTCQNYTRAYIRHLIKADETFGLRLTSYHNLYFLLNLMEKIRQAIMDDNILEFREDFIEKYGYGRSERNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pyogenes serotype M1
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.054 kDa
Sequence
MTDYPIKYRLIKAEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAIGSGIILSNTYHLWLRPGDELIARSGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVAMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVIKNAKFAEDFTPLDHDCDCYTCQNYSRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFRQDFLERYGYNKSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.121 kDa
Sequence
MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFSGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCNNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFREYFVEKYGYNKSGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.084 kDa
Sequence
MTDYPIKYRLIKTEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAIGSGIILSNTYHLWLRPGDELIARSGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVAMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVIKNAKFAEDFTPLDHDCDCYTCQNYSRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFRQDFLERYGYNKSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pneumoniae serotype 19F (strain G54)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.121 kDa
Sequence
MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFSGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCNNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFREYFVEKYGYNKSGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.1 kDa
Sequence
MTDYPIKYRLIKTEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAIGSGIILSNTYHLWLRPGDELIARSGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVAMDFLGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVIKNAKFAEDFTPLDHDCDCYTCQNYSRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFRQDFLERYGYNKSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.186 kDa
Sequence
MTKKRYTLLKKDGKARRGEFVTPHGTIQTPVFMNVGTLAAIKGAVSSMDLKEIGCQVELSNTYHLHLRPGDKIVKQMGGLHNFMNWDRPILTDSGGFQVFSLAGMRKIKEEGVYFNSHIDGRKIFMGPEESMQIQSNLGSTIAMAFDECIPNPSTREYVEKSVARTTRWLERCKKEMDRLNSLDDTVNKEQMLFGINQGGVYEDIRIEHAKTIREMDLDGYAIGGLAVGETHEEMYRVIDAVVPHLPEDKPIYLMGVGLPSNILEAVERGVDFFDCVLPARNGRHGHVFTKEGKINLMNAKFELDARPIDEGCQCPACKNYTRAYIRHLFKAKEMLAMRLCVLHNLYFYNKLMEDIRDAIDGGYFAEFKAKKLEEWNGRA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium perfringens (strain 13 / Type A)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.2 kDa
Sequence
MTKKRYTLLKKDGKARRGEFVTPHGTIQTPIFMNVGTLAAIKGAVSSMDLKEIGCQVELSNTYHLHLRPGDKIVKQMGGLHNFMNWDRPILTDSGGFQVFSLAGMRKIKEEGVYFNSHIDGRKIFMGPEESMQIQSNLGSTIAMAFDECIPNPSTREYVEKSVARTTRWLERCKKEMDRLNSLDDTVNKEQMLFGINQGGVYEDIRIEHAKTIREMDLDGYAIGGLAVGETHEEMYRVIDAVVPHLPEDKPIYLMGVGLPSNILEAVERGVDFFDCVLPARNGRHGHVFTKEGKINLMNAKFELDARPIDEGCQCPACKNYTRAYIRHLFKAKEMLAMRLCVLHNLYFYNKLMEDIRDAIDGGYFAEFKAKKLEEWNGRA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium perfringens (strain SM101 / Type A)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.186 kDa
Sequence
MTKKRYTLLKKDGKARRGEFVTPHGTIQTPVFMNVGTLAAIKGAVSSMDLKEIGCQVELSNTYHLHLRPGDKIVKQMGGLHNFMNWDRPILTDSGGFQVFSLAGMRKIKEEGVYFNSHIDGRKIFMGPEESMQIQSNLGSTIAMAFDECIPNPSTREYVEKSVARTTRWLERCKKEMDRLNSLDDTVNKEQMLFGINQGGVYEDIRIEHAKTIREMDLDGYAIGGLAVGETHEEMYRVIDAVVPHLPEDKPIYLMGVGLPSNILEAVERGVDFFDCVLPARNGRHGHVFTKEGKINLMNAKFELDARPIDEGCQCPACKNYTRAYIRHLFKAKEMLAMRLCVLHNLYFYNKLMEDIRDAIDGGYFAEFKAKKLEEWNGRA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Proteus mirabilis (strain HI4320)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.442 kDa
Sequence
MKYELDKTDGHARRGRLKFERGVVETPAFMPVGTYGTVKGMTPEEVEATGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGAMRKIKEEGVHFRNPINGEKIFLSPEKSMEIQYDLGSDIVMIFDECTPYPSDWDYAKNSMEMSLRWAKRSRQRFDELNNKNALFGIIQGGVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTNGVIKIRNAKHRSDTSTLDEHCDCYTCKNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAEIRQAIDESRFEDFVHEFYERIGKPVPPLNSSASKCD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.992 kDa
Sequence
MIDFPIKYRLIKKEKYTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELQQMGSGIILANTYHLWLRPGDELIAKAGGLHKFMNWDQAILTDSGGFQVYSLAEKRDISEEGVTFKNHLNGSKMFLSPEKAISVQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSSHDLVSMDFPGYSIGGLAVGETHEEMNAVLDFTVPLLPENKPRYLMGVGAPDSLIDGVIRGVDMYDCVLPTRIARNGTCMTSNGRLVVKNAAYAEDFSPIDPECDCYTCKNYTRAYVRHLLKADETFGIRLTSYHNLYFLVNLMAKVRQAIVDDNLLEFRQDFIEKYGYNASNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.992 kDa
Sequence
MIDFPIKYRLIKKEKYTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKQMGSGIILANTYHLWLRPGDELIAKAGGLHKFMNWDQAILTDSGGFQVYSLAEKRDISEEGVTFKNHLNGSKMFLSPEKAISVQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSSHDLVSMDFPGYSIGGLAVGETHEEMNAVLDFTVPLLPENKPRYLMGVGAPDSLIDGVIRGVDMYDCVLPTRIARNGTCMTSNGRLVVKNAAYAEDFSPIDPECDCYTCKNYTRAYVRHLLKADETFGIRLTSYHNLYFLVNLMAKVRQAIVDDNLLEFRQDFIEKYGYNASNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus uberis (strain ATCC BAA-854 / 0140J)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.075 kDa
Sequence
MTDYPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAMGSGIILSNTYHLWLRPGDELIAKAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVSMDFPGYSVGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFAEDFTPLDHDCDCYTCQNYTRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFREDFLERYGYNTSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pneumoniae (strain JJA)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.121 kDa
Sequence
MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFSGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCNNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFREYFVEKYGYNKSGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pneumoniae (strain P1031)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.086 kDa
Sequence
MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMLLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFSGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCNNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFRKYFVEKYGYNKSGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pneumoniae (strain Taiwan19F-14)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.12 kDa
Sequence
MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFSGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCNNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFRKYFVEKYGYNKSGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.83 kDa
Sequence
MEPAIKYRLIKKEKHTGARLGELITPHGTFPTPMFMPVGTQASVKSLAPEELDAMGAGVILSNTYHLWLRPGEQIVKEAGGLHQFMNWKKGILTDSGGFQVFSLAKNRDITEEGVHFKNHLNGSKMFLSPEKAIQIENDLGPDIMMSLDECPPFFESYDYVSKSVARTSRWAERGLKVHQHPDYQGLFGIVQGAGFKDLREQSAKDLVSLDFPGYSIGGLSVGESKAEMNHVLDFTTPLLPENKPRYLMGVGSADALIDGAIRGVDMFDCVLPTRIARNGTCMTSHGRLVVKNAAYAHDFTPLDDNCDCYTCRNFTRAYIRHLIKADETFGLRLTSYHNLYFLLHLMKQVRQAIMDDNLLEFRQNFFEMYGFNDKNPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Lactobacillus sakei subsp. sakei (strain 23K)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.85 kDa
Sequence
MEPAIKYRLIKKEKHTGARLGEIVTPHGTFKTPMFMPVGTQASVKTMAPEDLKEMGAGIILSNTYHLWLRPGEDIVEKAGGLHKFMNWDRGVLTDSGGFQVFSLAKLRDISEEGVAFKSHLNGEKLFLSPEKAIHVENALGADIMMSFDECPPFFESYDYVKKSVERTSRWAERGLIAHQNPATQGLFGIVQGAGFEDLRRQSARDLVGMDFPGYSIGGLSVGESKGEMNRVLDFTTPMLPEDKPRYLMGVGSPDALIDGVIRGVDMFDCVLPTRIARNGTTMTSQGRLVVKNAKYSEDFRPLDPKCDCYVCKNYTRAYIRHLIKADETFGIHLTSYHNLYFLINLMHQVQDAIEQDNLLEFREAFFEEYGYNENNGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pneumoniae (strain 70585)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.12 kDa
Sequence
MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFSGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCNNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFRKYFVEKYGYNKSGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pyogenes serotype M18 (strain MGAS8232)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.084 kDa
Sequence
MTDYPIKYRLIKTEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAIGSGIILSNTYHLWLRPGDELIARSGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVAMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVIKNAKFAEDFTPLDHDCDCYTCQNYSRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFRQDFLERYGYNKSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pyogenes serotype M12 (strain MGAS2096)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.084 kDa
Sequence
MTDYPIKYRLIKTEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAIGSGIILSNTYHLWLRPGDELIARSGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVAMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVIKNAKFAEDFTPLDHDCDCYTCQNYSRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFRQDFLERYGYNKSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pyogenes serotype M12 (strain MGAS9429)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.084 kDa
Sequence
MTDYPIKYRLIKTEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAIGSGIILSNTYHLWLRPGDELIARSGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVAMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVIKNAKFAEDFTPLDHDCDCYTCQNYSRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFRQDFLERYGYNKSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pyogenes serotype M2 (strain MGAS10270)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.084 kDa
Sequence
MTDYPIKYRLIKTEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAIGSGIILSNTYHLWLRPGDELIARSGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVAMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVIKNAKFAEDFTPLDHDCDCYTCQNYSRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFRQDFLERYGYNKSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pyogenes serotype M4 (strain MGAS10750)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.07 kDa
Sequence
MTDYPIKYRLIKTEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAIGSGIILSNTYHLWLRPGDELIARSGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVAMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFAEDFTPLDHDCDCYTCQNYSRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFRQDFLERYGYNKSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pyogenes serotype M5 (strain Manfredo)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.084 kDa
Sequence
MTDYPIKYRLIKTEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAIGSGIILSNTYHLWLRPGDELIARSGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVAMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVIKNAKFAEDFTPLDHDCDCYTCQNYSRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFRQDFLERYGYNKSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pneumoniae (strain Hungary19A-6)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.145 kDa
Sequence
MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFPGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCKNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFREYFVEKYGYNKSGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.121 kDa
Sequence
MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFSGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCNNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFREYFVEKYGYNKSGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pyogenes serotype M28 (strain MGAS6180)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.084 kDa
Sequence
MTDYPIKYRLIKTEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAIGSGIILSNTYHLWLRPGDELIARSGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVAMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVIKNAKFAEDFTPLDHDCDCYTCQNYSRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFRQDFLERYGYNKSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.121 kDa
Sequence
MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFSGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCNNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFREYFVEKYGYNKSGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pyogenes serotype M3 (strain SSI-1)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.084 kDa
Sequence
MTDYPIKYRLIKTEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAIGSGIILSNTYHLWLRPGDELIARSGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVAMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVIKNAKFAEDFTPLDHDCDCYTCQNYSRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFRQDFLERYGYNKSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pneumoniae (strain CGSP14)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.121 kDa
Sequence
MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFSGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCNNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFREYFVEKYGYNKSGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pyogenes serotype M49 (strain NZ131)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.07 kDa
Sequence
MTDYPIKYRLIKTEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKAIGSGIILSNTYHLWLRPGDELIARSGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVAMDFPGYSIGGLAVGESHEEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFAEDFTPLDHDCDCYTCQNYSRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFRQDFLERYGYNKSNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.121 kDa
Sequence
MSDSPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEMGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFSGYSIGGLAVGETHEEMNAVLDFTTQLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSQGRLVVKNAQFAEDFTPLDPECDCYTCNNYTRAYLRHLLKADETFGIRLTSYHNLYFLLNLMKQVRQAIMDDNLLEFREYFVEKYGYNKSGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus suis (strain 98HAH33)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.037 kDa
Sequence
MTDVPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTMSPEELKAMGSGIILSNTYHLWLRPGDELVARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNISEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFPGYSIGGLAVGETHDEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTNRGRLVVKNAQFAEDFTPLDPECDCYTCKNYTRAYLRHLLKADETFGIRLTSYHNLYFLINLMKNVRQAIMDDNLLEFRQDFMEKYGYGKNGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus equi subsp. zooepidemicus (strain H70)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.999 kDa
Sequence
MTNYPITYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKEIGSGIILSNTYHLWLRPGDELIARAGGLHKFMNWDQAILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAADLVGMDFPGYSIGGLAVGESHAEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFAEDFTPLDHNCDCYTCQHYTRAYLRHLLKADETFGMRLTSYHNLYFLVNLMKQVRQAIMDDNLLEFRQDFLERYGYNSSSRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus sanguinis (strain SK36)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.036 kDa
Sequence
MSTSPIQYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELKQMGSGIILANTYHLWLRPGDELIARAGGLHTFMNWDQPILTDSGGFQVYSLADSRNITEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHSRPHDQGLFGIVQGAGFEDLRRQSAQDLVSMDFPGYSIGGLAVGESHEEMNAVLDFTTPMLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSEGRLVVKNAQFEEDFTPLDHDCDCYTCSNYTRAYIRHLLKADETFGIRLTSYHNLYFLVNLMKKVRQAIMDDNLLEFREDFIERYGYNKSSRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus suis (strain 05ZYH33)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.037 kDa
Sequence
MTDVPIKYRLIKKEKHTGARLGEIITPHGTFPTPMFMPVGTQATVKTMSPEELKAMGSGIILSNTYHLWLRPGDELVARAGGLHKFMNWDQPILTDSGGFQVYSLADSRNISEEGVTFKNHLNGSKMFLSPEKAISIQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSAHDLVSMDFPGYSIGGLAVGETHDEMNAVLDFTTPLLPENKPRYLMGVGAPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTNRGRLVVKNAQFAEDFTPLDPECDCYTCKNYTRAYLRHLLKADETFGIRLTSYHNLYFLINLMKNVRQAIMDDNLLEFRQDFMEKYGYGKNGRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Streptococcus thermophilus (strain CNRZ 1066)
Length
380 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.02 kDa
Sequence
MIDFPIKYRLIKKEKYTGARLGEIITPHGTFPTPMFMPVGTQATVKTQSPEELQQMGSGIILANTYHLWLRPGDELIAKAGGLHKFMNWDQAILTDSGGFQVYSLAEKRDISEEGVTFKNHLNGSKMFLSPEKAISVQNNLGSDIMMSFDECPQFYQPYDYVKKSIERTSRWAERGLKAHRRPHDQGLFGIVQGAGFEDLRRQSSHDLVSMDFPGYSIGGLAVGETHEEMNAVLDFTVPLLPENKPRYLMGVGAPDSLIDGVIRGVDMYDCVLPTRIARNGTCMTSNGRLVVKNAAYAEDFSPIDPECDCYTCKNYTRAYVRHLLKADETFGIRLTSYHNLYFLVNLMARVRQAIVDDNLLEFRQDFIEKYGYNASNRNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.915 kDa
Sequence
MNPITYELIKTDKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEDLQSMQANIILSNTYHLWLRPGEDIIREAGGLHKFMNWDGAILTDSGGFQVFSLSDMREIKEEGVHFRNHLNGEKLFLSPEKAMDIQNALGSDIMMAFDECPPYPAEYDYMKASVERTSRWAERCLQAHNRPHDQGLFGIVQGGEYEALRKQSAEDLVSLDFPGYAIGGLSVGEPKHVMNKVLEFTTPFLPSNKPRYLMGVGSPDALIDGAIRGVDMFDCVLPTRIARNGTCMTSNGRLVVRNAKYARDFNPIDEHCSCHVCKNYSRAYIRHLIKCNETFGFRLTTYHNLHFLLKLMEQVRTAIKEDRLGDFKESFFEQYGLNKANPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / 130Z)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.385 kDa
Sequence
MKFKLKTTSGTARRGEMTFSRPQGEFTVQTPAFMPVGTYGTVKGMTPEEVRATGAEILLGNTFHLWLRPGQEVMRKHGDLHDFMQWHRPILTDSGGFQVFSLGKLRKITEEGVKFQNPINGERIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKKSMEMSLRWAQRSRDRFDELGNKNALFGIVQGGTFEELRKVSAEGLVDIGFDGYAVGGLAVGEPKEEMHRILEFTTPLLPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGIVKIRNAKYRDDTSALDPHCDCYTCRHYTKSYLYHLDKCGEILGARLNTIHNLRYYQRLMEEIRQAIEEDRFDDFVVEFYTRMGKEVPPLQKP

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Anoxybacillus flavithermus (strain DSM 21510 / WK1)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.161 kDa
Sequence
MTPIRYELIKTCKQTGARLGILHTPHGSFETPMFMPVGTLATVKTLSPEELKEMGAGVILSNTYHLWLRPGHDIVKEAGGLHSFMNWDRGILTDSGGFQVFSLSEFRRIEEEGVYFRNHLNGDQLFLSPEKAMEIQNALGSDIMMAFDECPPYPATYEYMKRSVERTSRWAERCLKAHQRPNEQGLFGIVQGGEFEDLRKQSAQDLVSLDFPGYAVGGLSVGEPKEVMNRVLEFTTPLLPANKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIGRNGTVMTSEGRVVIKNAKYARDFTPLDPNCDCYTCRNYTRAYIRHLIKCDETFGIRLTSYHNVYFLIKLMEQVRQAIREDRLGDFREQFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Solibacter usitatus (strain Ellin6076)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.674 kDa
Sequence
MPQISFEVVAECPHTRARAGVLHTAHGDIETPVFMPVGTQATVKGLTQRDLAEDLGVKILLSNTYHLYLRPGHELIRQMGGLHKFMSWPNAILTDSGGFQVFSLSGLRKIHEHGVVFQSHLNGDTHKFTPESTVDVQLAYGSDILMVLDECPEYPVSHEYARESMQRTVRWAREANEHFLERMKQMPTRHALFPIVQGSMFTDLRRECATALVDLDTDGYAIGGLSVGEPRPLSLEVVEATEAILPRTKPRYAMGVGMPAELPEYVARGIDMMDCVLPSRNARNGYLFTSEGRVIIKHARYKDDEGPLDPRCACYTCKSYSRAYLRHLFQSGEILFSVLATRHNIQRYLDIMREIRHAIISGSFPDYLRCVQSSLHDAG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain Mu3 / ATCC 700698)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain JH1)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain USA300)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain NCTC 8325)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain JH9)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.284 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEHEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain COL)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain Newman)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain N315)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain MRSA252)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.074 kDa
Sequence
MKEKKEIFTLLHQDAASPARTGVLELPHGKVLTPAFMPVGTAATVKAMTKDDLDEIGFEIILANTYHLFLRPGIEVIKAAGGLHGFSDWKKNFLTDSGGFQVFSLSQLRKITEEGVKFQSHIDGSRQFLSPEIAVELQTGFNSDIQMQLDICSSFGISKTQTLADLKITMNWLDRAFAAWHNTPHEYDGALFPIVQGGFFEDLRLQSLEAILKHEPRGIAIGGLSIGEPKDLYQEYLSFTAKHIPKNKPLYVMGIGTPDYILEAVKNGVDIFDCVLPSRNARNGNLFTHEGAISIKRKEYEFDFNPIDSQCKCKVCRQYTRAYLRHLFRTKEILYSMLATYHNLAFLYSMVQDIREAIQNDSFNDYYKNFLKKYENRLD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.269 kDa
Sequence
MKLKFELKKKNGNARRGQLIFERGTVQTPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEVMKMHGDLHDFMNWQGPILTDSGGFQVFSLGDIRKITEEGVHFRNPVNGDKIFMDAEKSMEIQKDLGSDIVMIFDECTPYPATHDEAKKSMEMSLRWAKRSRDHFDKLENPNNLFGIVQGGVYEDLRDVSVKGLTEIGFDGYAVGGLAVGEPKEDMHRVLEHTCPQLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGVIKIRNAAHKTDTTPLDLHCDCYTCKNYSKSYLHHLDRCNEILGARLNTIHNLRYYQRLMESIRKAIDEDRFDQFVAEFYARRNREVPPLQKDKA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.253 kDa
Sequence
MKLKFELKKKNGNARRGQLIFERGTVQTPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEVMKMHGDLHDFMNWQGPILTDSGGFQVFSLGDIRKITEEGVHFRNPVNGDKIFMDAEKSMEIQKDLGSDIVMIFDECTPYPATHDEAKKSMEMSLRWAKRSRDHFDKLENPNNLFGIVQGGVYEDLRDVSVKGLTEIGFDGYAVGGLAVGEPKEDMHRVLEHTCPQLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGVIKIRNAAHKTDTTPLDPHCDCYTCKNYSKSYLHHLDRCNEILGARLNTIHNLRYYQRLMESIRKAIDEDRFDQFVAEFYARRNREVPPLQKDKA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Vibrio cholerae serotype O1 (strain M66-2)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.253 kDa
Sequence
MKLKFELKKKNGNARRGQLIFERGTVQTPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEVMKMHGDLHDFMNWQGPILTDSGGFQVFSLGDIRKITEEGVHFRNPVNGDKIFMDAEKSMEIQKDLGSDIVMIFDECTPYPATHDEAKKSMEMSLRWAKRSRDHFDKLENPNNLFGIVQGGVYEDLRDVSVKGLTEIGFDGYAVGGLAVGEPKEDMHRVLEHTCPQLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGVIKIRNAAHKTDTTPLDPHCDCYTCKNYSKSYLHHLDRCNEILGARLNTIHNLRYYQRLMESIRKAIDEDRFDQFVAEFYARRNREVPPLQKDKA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain MSSA476)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain USA300 / TCH1516)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus aureus (strain MW2)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKITEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKKSIERTTRWAKRCLDAHQRPEDQALFGIIQGGEYEDLREQSAKDLVELDFPGYAIGGLSVGEPKPVMYKMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSQGRLVIKNAKFADDLRPLDENCDCYTCQNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKEEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.121 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRNIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKISEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKDSIERTTRWAARCLKAHQRPGDQALFGIIQGGEYKDLREQSAKELVSLDFPGYAIGGLSVGEPKPVMYDMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSNGRLVVKNAKYADDLRPLDEQCDCYTCQHYTRAYIRHLVKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKDEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus epidermidis (strain ATCC 12228)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.121 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRNIEAKIILGNTYHLWLQPGNDIIKHAGGLHKFMNWDGPILTDSGGFQVFSLSNLRKISEEGVEFRHHTNGSKLFLSPEKSMQIQNDLGSDIMMAFDECPPMPAEYDYVKDSIERTTRWAARCLKAHQRPGDQALFGIIQGGEYKDLREQSAKELVSLDFPGYAIGGLSVGEPKPVMYDMVEHTEQFMPKDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSNGRLVVKNAKYADDLRPLDEQCDCYTCQHYTRAYIRHLVKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKDEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Staphylococcus haemolyticus (strain JCSC1435)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.31 kDa
Sequence
MPAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTKATVKTMSPEELRQIEAKIILGNTYHLWLQPGNDIIKQVGGLHNFMNWDGPILTDSGGFQVFSLSNLRKITEESVEFRHHTNGLKLFLSPEKSMEIQNDLGSDIMMAFDECPPMPSEYKYVKDSIERTTRWAERCLNAHKRPEDQALFGIIQGGEYKDLREQSAKELVALDFPGYAIGGLSVGEPKPVMYEMVEHTVQYMPDDKPRYLMGVGSPDALIECSIRGMDMFDCVLPTRIARNGTCMTSNGRLVIKNAKYANDFKPLDENCDCYTCKNYSRAYIRHLIKAEETFGIRLTTIHNLHFLLKLMEDIRQAIREDRLLDFKDEFFEQYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus anthracis (strain A0248)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.227 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus anthracis (strain CDC 684 / NRRL 3495)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.227 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus thuringiensis (strain Al Hakam)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.227 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus anthracis
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.227 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus cereus (strain AH820)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.227 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus cereus (strain ATCC 10987 / NRS 248)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.227 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus cereus (strain G9842)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.243 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEYEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus cereus (strain 03BB102)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.227 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus cereus (strain B4264)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.243 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEYEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus cereus (strain AH187)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.227 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.266 kDa
Sequence
MTAIRYEFIKKCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIVREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVYFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLNAHQRPEDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPENKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSQGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus cereus (strain Q1)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.213 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIVREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.243 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEYEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus cereus (strain ZK / E33L)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.227 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Edwardsiella ictaluri (strain 93-146)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.846 kDa
Sequence
MKYELVSTDGRARRGRLIFERGVVETPAFMPVGTYGTVKGMTPEEVAQTGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWPGPILTDSGGFQVFSLGAMRKIKEEGVYFRNPINGSPVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRQRFDELGNQNALFGIIQGSVYEDLRDVSLKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPMIPQDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGVVKIRNAQYKEDTTALDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAALRQAIEEGKLERFAADFYGRRGRTVPPLGAADAAS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Listeria monocytogenes serotype 4a (strain HCC23)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.951 kDa
Sequence
MSAIRYELIKTDKQTGARLGKIHTPHGTFDTPMFMPVGTLATVKTMSPEELKAMGAGIILSNTYHLWLRPGEELIREAGGLHKFMNWDQPILTDSGGFQVFSLSKMRDIKEEGVHFRNHLNGDKLFLSPEKAIQIQNALGSDIMMSFDECPPYPASHEYMKKSVERTSRWAERGLKAHERPEDQGLFGIVQGGAYEDLRAQSAKDLVSLDFPGYSIGGLSVGEPKDVMNRVLEHTTPLLPANKPRYLMGVGSPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSSGRLVIKNAKFTHDFRPIDENCDCYTCKNYSRAYIRHLIRCEETFGIRLTTYHNLHFLLNLMKQVRGAIMEDRLADFREEFFEQYGFNRPDAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.921 kDa
Sequence
MSAIRYELIKTDKQTGARLGKIHTPHGTFDTPMFMPVGTLATVKTMSPEELKAMGAGIILSNTYHLWLRPGEELIREAGGLHKFMNWDQPILTDSGGFQVFSLSKMRDIKEEGVHFRNHLNGDKLFLSPEKAIQIQNALGSDIMMSFDECPPYPASHEYMKKSVERTSRWAERGLKAHVRPEDQGLFGIVQGGAYEDLRAQSAKDLVSLDFPGYSIGGLSVGEPKDVMNRVLEHTTPLLPANKPRYLMGVGSPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSSGRLVIKNAKFTHDFRPIDENCDCYTCKNYSRAYIRHLIRCEETFGIRLTTYHNLHFLLNLMKQVRGAIMEDRLADFREEFFEQYGFNRPDAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.923 kDa
Sequence
MSAIRYELIKTDKQTGARLGKIHTPHGTFDTPMFMPVGTLATVKTMSPEELKAMGAGIILSNTYHLWLRPGEELIREAGGLHKFMNWDQPILTDSGGFQVFSLSKMRDIKEEGVHFRNHLNGDKLFLSPEKAIQIQNALGSDIMMSFDECPPYPASHEYMKKSVERTSRWAERGLQAHARPEDQGLFGIVQGGAYEDLRAQSAKDLVSLDFPGYSIGGLSVGEPKDVMNRVLEHTTPLLPANKPRYLMGVGSPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSSGRLVIKNAKFTHDFRPIDENCDCYTCKNYSRAYIRHLIRCEETFGIRLTTYHNLHFLLNLMKQVRSAIMEDRLADFREEFFEQYGFNRPDAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Macrococcus caseolyticus (strain JCSC5402)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.194 kDa
Sequence
MNAVTYEHIKTCKQSGARLGIVHTPHGSFETPMFMPVGTQATVKTMSPEELKAMNAKIILSNTYHLWLRPGNDVIREAGGLHKFMNWDGPILTDSGGFQVFSLSDMRKIEEEGVHFRHHLNGSKLFLSPHKAMHIQNDLGSDIMMAFDECPPMPATYEYVKASIERTSRWAERCLEAHQRPEDQALFGIIQGGEYEDLRTQSAKDLVSMDFPGYAIGGLSVGEPKPIMYRMLEHTTPLMPFNKPRYLMGVGSPDALIEGAIRGIDMFDCVLPTRIARNGTCMTSKGRVVVKNAKYERDFTPLDEKCECYTCKNYTKAYLRHLIKADETFGIRLTTIHNLHFLLNLMEQVREAIRNDRLLDFKEEFFEEYGLNVENPKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Mannheimia succiniciproducens (strain MBEL55E)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.36 kDa
Sequence
MKFKLKTTSGAARRGELTFNRPQGEFSVQTPAFMPVGTYGTVKGMTPEEVRATGAEILLGNTFHLWLRPGQEVMRKHGDLHDFMQWHRPILTDSGGFQVFSLGKLRKITEEGVKFQNPINGERIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKKSMEMSLRWAKRSRDRFDELGNKNALFGIVQGGTFEELRKVSAENLINIGFDGYAVGGLAVGEPKEEMHRILEFTTPLLPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGIVKIRNAKYKDDTSPLDPHCDCYTCQHYTKSYLYHLDKCGEILGARLNTIHNLRYYQRLMEQIRTAIEQDRFDDFVQEFYARMDKPVPPLQKA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.062 kDa
Sequence
MAAVTYELIKTCKQSGARLGKLHTPHGTIETPIFMPVGTLATVKTMSPEELKQLGAQIILSNTYHLWLRPGHDIVKEAGGLHEFMNWDRPILTDSGGFQVFSLSDLRTIEEEGVHFRNHLSGEKLFLSPEGAMEIQNALGSDIMMAFDECPPYPAERDYMRPSVERTSRWAERCLKAHKRPEDQALFGIIQGGEYEDLRRQSAQDITSLDFPGYAIGGVSVGEPKDVMNRVLEFTTPLLPANKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSNGRLVVRNAKYARDFRSLDENCDCHVCQTYTRAYIRHLVKCDETFGFRLTTYHNLYFLLKLMKDVRQAILDDRLLDFREEFFEQYGFNQPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus thuringiensis subsp. konkukian (strain 97-27)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.227 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIIREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAVGGLSVGEPKDIMNRVLEFTTPLLPDNKPRYLMGVGSPDSLIDGAIRGIDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Bacillus weihenstephanensis (strain KBAB4)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.214 kDa
Sequence
MTAIRYEFIKTCKQTGARLGRVHTPHGSFDTPTFMPVGTLATVKTMSPEELKAMDSGIILSNTYHLWLRPGHEIVREAGGLHKFMNWDRAILTDSGGFQVFSLSDFRRIEEEGVHFRNHLNGDKLFLSPEKAMEIQNALGSDIMMAFDECPPFPATFEYMKKSVERTSRWAERCLKAHERPQDQGLFGIVQGGEFEELRRQSAKDLVSMDFPGYAIGGLSVGEPKDIMNRVLEFTTPLLPDDKPRYLMGVGSPDSLIDGAIRGVDMFDCVLPTRIARNGTCMTSEGRLVVKNAKFARDFGPLDPNCDCYTCKNYSRAYIRHLMKCDETFGIRLTSYHNLHFLLNLMEQVRQAIREDRLGDFREEFFEQYGFNKPNAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.981 kDa
Sequence
MSAIRYELIKTDKQTGARLGKIHTPHGTFDTPMFMPVGTLATVKTMSPEELKAMGAGIILSNTYHLWLRPGEELIREAGGLHKFMNWDQPILTDSGGFQVFSLSKMRDIKEEGVHFRNHLNGDKLFLSPEKAIQIQNALGSDIMMSFDECPPYPASHEYMKKSVERTSRWAERGLKAHERPEDQGLFGIVQGGAYEDLRAQSAKDLVSLDFPGYSIGGLSVGEPKDVMNRVLEHTTPLLPANKPRYLMGVGSPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSSGRLVIKNAKFTHDFRPIDENCDCYTCKNYSRAYIRHLIRCEETFGIRLTTYHNLHFLLNLMKQVRSAIMEDRLADFREEFFEQYGFNRPDAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Listeria monocytogenes serotype 4b (strain CLIP80459)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.921 kDa
Sequence
MSAIRYELIKTDKQTGARLGKIHTPHGTFDTPMFMPVGTLATVKTMSPEELKAMGAGIILSNTYHLWLRPGEELIREAGGLHKFMNWDQPILTDSGGFQVFSLSKMRDIKEEGVHFRNHLNGDKLFLSPEKAIQIQNALGSDIMMSFDECPPYPASHEYMKKSVERTSRWAERGLKAHVRPEDQGLFGIVQGGAYEDLRAQSAKDLVSLDFPGYSIGGLSVGEPKDVMNRVLEHTTPLLPANKPRYLMGVGSPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSSGRLVIKNAKFTHDFRPIDENCDCYTCKNYSRAYIRHLIRCEETFGIRLTTYHNLHFLLNLMKQVRGAIMEDRLADFREEFFEQYGFNRPDAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Listeria monocytogenes serotype 4b (strain F2365)
Length
379 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.921 kDa
Sequence
MSAIRYELIKTDKQTGARLGKIHTPHGTFDTPMFMPVGTLATVKTMSPEELKAMGAGIILSNTYHLWLRPGEELIREAGGLHKFMNWDQPILTDSGGFQVFSLSKMRDIKEEGVHFRNHLNGDKLFLSPEKAIQIQNALGSDIMMSFDECPPYPASHEYMKKSVERTSRWAERGLKAHVRPEDQGLFGIVQGGAYEDLRAQSAKDLVSLDFPGYSIGGLSVGEPKDVMNRVLEHTTPLLPANKPRYLMGVGSPDSLIDGVIRGVDMFDCVLPTRIARNGTCMTSSGRLVIKNAKFTHDFRPIDENCDCYTCKNYSRAYIRHLIRCEETFGIRLTTYHNLHFLLNLMKQVRGAIMEDRLADFREEFFEQYGFNRPDAKNF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Vibrio vulnificus (strain CMCP6)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.1 kDa
Sequence
MKLKFDLKKKNGNARRGQLTFERGTVQTPAFMPVGTYGTVKGMTPEEVKETGAEILLGNTFHLWLRPGQEVMKMHGDLHDFMNWQGPILTDSGGFQVFSLGDIRKITEEGVHFRNPVNGDKIFMDAEKSMEIQKDLGSDIVMIFDECTPYPATHAEAKKSMEMSLRWAQRSRDHFDKLENPNNLFGIVQGGVYEDLRDVSVKGLTEIGFDGYAVGGLAVGEPKEDMHRVLEHTCPQLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGVIKIRNATHKTDTTPLDPHCDCYTCKNYSKSYLHHLDRCNEILGARLNTIHNLRYYQRLMESIRKAIDEDRFEQFVEEFYARRNREVPPLGKQA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Vibrio vulnificus (strain YJ016)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.1 kDa
Sequence
MKLKFDLKKKNGNARRGQLTFERGTVQTPAFMPVGTYGTVKGMTPEEVKETGAEILLGNTFHLWLRPGQEVMKMHGDLHDFMNWQGPILTDSGGFQVFSLGDIRKITEEGVHFRNPVNGDKIFMDAEKSMEIQKDLGSDIVMIFDECTPYPATHAEAKKSMEMSLRWAQRSRDHFDKLENPNNLFGIVQGGVYEDLRDVSVKGLTEIGFDGYAVGGLAVGEPKEDMHRVLEHTCPQLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGVIKIRNATHKTDTTPLDPHCDCYTCKNYSKSYLHHLDRCNEILGARLNTIHNLRYYQRLMESIRKAIDEDRFEQFVEEFYARRNREVPPLGKQA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.029 kDa
Sequence
MKYELQKTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWHGPILTDSGGFQVFSLGAMRKIKEEGVTFQNPINGDKVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDELNNKNALFGIIQGGVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTATLDEHCDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMASLRQAIEEGKLESFVEYFYGRIGKPVPPLSPQLTD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.001 kDa
Sequence
MKFELKTTDGRARRGQLVFERGTVQTPAFMPVGTYGTVKGMTPEEVRETGAQILLGNTFHLWLRPGQEVMRAHGDLHDFMNWQGPILTDSGGFQVFSLGHIRKITEAGVHFRHPINGEKIFLDPEKSMEIQYDLGSDIVMIFDECTPYPATYEEARKSMEMSLRWGKRSRDKFDALGNKNALFGIIQGSVYEDLRDVSLDGLLEIGFDGYAVGGLAVGEPKEDMHRILEHVCPKIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFTTDGVVKIRNAKYREDTSTLDADCDCYTCKNYTRSYLYHLDKCNEILGARLNTIHNLRYYQRVMQGLRDAIEQGKLDDFVTEFYRRQGKPVPPLAENDVK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Aeromonas salmonicida (strain A449)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.959 kDa
Sequence
MKFELKTTDGRARRGQLVFERGTVQTPAFMPVGTYGTVKGMTPEEVRETGAEILLGNTFHLWLRPGQEVMRAHGDLHDFMNWQGPILTDSGGFQVFSLGHIRKITEAGVHFRHPINGEKIFLDPEKSMEIQYDLGSDIVMIFDECTPYPATYEEARKSMEMSLRWGKRSRDKFDALGNKNALFGIIQGSVYEELRDVSLNGLLEIGFDGYAVGGLAVGEPKEDMHRILEHVCPKIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTTDGVVKIRNAKYRSDTSTLDADCDCYTCKNYTRSYLYHLDKCNEILGARLNTIHNLRYYQRVMQGLRDAIEQGKLDDFVTEFYRRQGKPVPPLAENDVK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Gloeobacter violaceus (strain ATCC 29082 / PCC 7421)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.054 kDa
Sequence
MTASFAFTIEHRDGEARAGTFATPHGPVYTPCFMPVGTQATVKTLTPAQLAETGAQMILANTYHLSLQPGADIVAGAGGLHGFMQWPGPILTDSGGFQVFSLSSLRTIDDDGVTFREPKSGALVRFTPEHAVAVQNALGADVIMAFDECPPYPADREQVEGAVERTLRWFERCVEAHRRSDQALFGIVQGGVWPDLRRRCAEGLVAADLPGYAIGGVSVGEPQTLIERVVRVTAPLLPEHKPRYLMGVGTFREMAQAVAVGVDLFDCVMPTRVARHGSALLLGTGGDRRINLKNAQFRRDYEPLDCVCPCYTCRHFSRAYLAHLVRSEEILAMTLLSIHNVATLTRFAALLRCAIATGSFAQEFAHYLQSGPEPVLSN

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.166 kDa
Sequence
MKLSFDLKKKNGNARRGQLTFERGTVQTPAFMPVGTYGTVKGMTPEEVKGTGAEILLGNTFHLWLRPGQEVMKMHGDLHDFMNWHGPILTDSGGFQVFSLGKMRKITEKGVHFRSPVNGDKIFMDAEKSMEIQKDLGSDIVMIFDECTPYPATHNEAKKSMEMSLRWAQRSRDHFDKLENPNNLFGIVQGGVYEDLRDVSIKGLTEIGFDGYAVGGLAVGEPKEDMHRILEHTCPQLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGVIKIRNAKHKTDTTPLDPHCDCYTCQHYSKSYLHHLERCNEILGARLNTIHNLRYYQRLMESIRKAIDEDRFDEFVTEFYERRGREVPPLAKEQ

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Vibrio tasmaniensis (strain LGP32)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.993 kDa
Sequence
MKLKYELKKTNSGARRGQLQFERGTVETPAFMPVGTYGTVKGMTPEEVKDTGAEILLGNTFHLWLRPGQEIMKLHGDLHDFMNWKGPILTDSGGFQVFSLGATRKITEEGVHFRNPVNGDKIFMDAEKSMEIQKDLGSDIVMIFDECTPYPATHKEAKDSMEMSLRWAQRSRDHFDKQENPNSLFGIVQGGVYEDLRDVSVKGLTEIGFDGYAVGGLAVGEPKEDMHRILEHTCPQLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTEGVIKIRNAKHKTDTTPLDSDCDCYTCKNYSKSYLHHLDRCNEILGARLNTIHNLRFYQRVMSDIRQSIDEDRFEEFVAEFYARMGREVPPLGKES

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Aquifex aeolicus (strain VF5)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.654 kDa
Sequence
MFKFHLITKDGKARRGRIYTPHGVIETPVFMPVGTQGTVKAMLHKLLDEIGTQIILGNTYHLYLRPGTEIIKKAGGLHRFISWNKPILTDSGGYQVFSLAKGKFGNRKAKVKVSDEGVEFQDHLQGDKHFFTPEKVVEIQEIFGSDIMMPLDECVEYPVDKNYAEKALKRTINWLERSIKAKKREDQVLFGIVQGAFWKDLRKKAVEETLKFDEFLFGYSIGGLSVGEPKEIMYGMTEVVCELLPEKKPRYLMGVGKPEDILEAVERGVDMFDCVVPTRNARTGTLYTSQGVVDIRHSKWKEDFSPLDPECDCYTCRNFSKAYLRHLFVAEEISAYVLNTIHNLRFYLKMMEEVRKAIEEKRFKELKEKYLQRVKNKL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Eubacterium eligens (strain ATCC 27750 / VPI C15-48)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.663 kDa
Sequence
MYKILKTDGRAKRAEFTTVHGTVQTPVFMNVGTVAAIKGAVATTDLQQIGTQIELSNTYHLHVRPGDKIIKQLGGLHKFMNWDKPILTDSGGFQVFSLAGLRKIKEEGVTFQSHIDGHKIFMGPEESMQIQSNLGSTIAMAFDECAPAKADRKYIQNSVDRTYRWLERCKKEMARLNSLPDTVNPDQMLFGIDQGGVFNDIRIDHAKRISELDLDGYAVGGLAVGETHEEMYDVLDNVVPYLPQDKPTYLMGVGTPANILESVDRGIDFFDCVYPSRNGRHGHVYTKFGKINLFNAKYETDTAPIEEGCGCPCCQNYSRAYVRHLLKAKEMLGMRLCVLHNLYYYNHLMTDIRAAIEEGRYAGFKEEALYQMKTYDKQ

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Methylacidiphilum infernorum (isolate V4)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.585 kDa
Sequence
MKFEVIQKSGGSRARLGRLLTPHGVVETPCFMPVGTSATVKAIFPKDLEEEGIKLILANAYHLLFRPGISVIKEFGGLHQFMGWNGAILTDSGGFQVFSLSPFCKIFPEGVRFKSPVDGSFLMLTPESAIHAQMELGSDIVMSLDHCPPWPSKEKDLLEATRRTIQWAKRGKETWMQQQEKLFSKPSASYSLFGIIQGGTDERLRLYCSEELMKIGFDGYAIGGLSVGEPHEESLAVVKTVSSFLDEKAPKYVMGMGQPWQIVQMVDLGIDLFDCVLPTRLARHGSAYVEEGIIHIKNARFRKDGSPLDSRCSCYACRKFSRGYIHHLLKSKEILGIMLLSMHNLLFYNRLMKEIRSFLAHGQWVDFLARWKDKKVTK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.264 kDa
Sequence
MEFRIDSIDGNARACTIKTEHSEIKTPIFMPVGTAAAVKSLDAIDMMEILDAPIILGNTYHLYLRPGDEIISKLGGLHGFSGYKRSFLTDSGGFQAFSLGDNVKFTDEGIWFKSHIDGSKHFFSPEKVIDIEYNLNSDIMMVLDDLIALPNTKERIKKSIERTTEWAYRSLVHHVNRGKKNNLFAIIQGGTDFEFRRISAESLVSLEYKGYTFDGFAIGGLSVGEENQLMYDTIEATTPYMPKDKPRYLMGVGTPEDIIEAVERGVDMFDCVMPTRNARNGYLFTTFGTLRIKNAKYKLDESPIDPKCNCYTCRNFSRAYLNHLFKAKELTYFRLASIHNLHYYLNFVKEIREAILEGRFKEYKKEFYSLRAMNSLEI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thermosynechococcus elongatus (strain BP-1)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.701 kDa
Sequence
MFEFVCQQECAHTQARAGLFHTPHGTVATPRFMPVGTLANVKTLTPEHLKAAGAQMILANTYHLHLQPGEDIVAAAGGLHCFMGWSGPILTDSGGFQVFSLSEMRQISDQGVVFRSPHDGQIIELSPEGAIAIQEALGADVIMAFDECPPYPASREAVIQATQRTLQWLERCIVAKQRSDQALFAIVQGGVYADLRRECAEAMVPYDLPGYAIGGVSVGEPNRIMHEIVAVTAPLLPVHKPRYLMGVGTHLEMLRAIAAGVDLFDCVIPTRLARHGCAIVQGQRWNLKNARFRRDYEPLDPTCPCYTCRTFSRAYLSHLVRAKELLAYTLLSIHNVTELIRFTQAARQAILEERFAAFAAEWEQRLVVDAEEPDAALL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Blochmannia floridanus
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.608 kDa
Sequence
MVFRVLQTDGDARVGKLTCHHGIIETPAFIPVGTYGVVKSVTSQEVAESGAQIILSNTFHLWLRPGLEIIKIHQNLHKFMNWMGPIITDSGGFQVFSLNKLRKITESGVYFKDPVNGSTIFLTPEKSMDIQYHLGSDIVLVFDECVSYPSTWEYIKNSVEISLNWAERSRLHFDKLHNSNMLFAIIQGGMYEELRNRSAQELINIKFDGYAIGGLSVGETPQERFRIVSYVCKIIPFDKPRYLMGVGKPQDLIEAVCLGVDMFDCVIPTRNARNGYLFTNNGVVRIRNAKYESDLDPIEEDCDCYTCQRYYSRSYLHYLDRCNESLGIRLNTIHNLRYYQRLMEEIRQSIRMKKLRKFVEAFNYKFNSVSTNNYLSNI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
Length
378 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.718 kDa
Sequence
MYKLICKDGNAKRGEFTTVHGKIQTPVFMNVGTAAAIKGAVSTMDLQEIGTQVELSNTYHLHVRPGDEVVKKLGGLHKFMVWDKPILTDSGGFQVFSLAGLRKIKEEGVYFNSHIDGKKIFMGPEESMRIQSNLASTIAMAFDECPPHPATREYMEDSVARTTRWLLRCKNEMNRLNTLEDTINKHQMLFGINQGGTYTDIRVEHAKRISELDLDGYALGGLAVGESHSEMYRIIEETVPYLPEAKPTYLMGVGTPANILEAVERGVDFFDCVYPARNGRHGHAYTNHGKMNLLNAKYELDDRPIEEGCGCPVCKNYSRGYIRHLLKAKEMLGLRFLVTHNLYFYNKMMEEIREAIENQNFASYKKKKLEGFAAEQGN

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.638 kDa
Sequence
MNFTLHVTDGRARAATLELAHGSIPTPIFMPVGTQASVKALDHTDLLEHIDAPIILGNTYHLYLRPGDENIAKLGGLHGFTKFPRNFLTDSGGFQAFSLNTNTKHSEEGIIFKSHIDGSKHLFTPEKVLEIEYNLNSDIMMVLDDLVGLPAPRERIKESIERTTRWAERSLLFHQAQKEQGKALTNHLFAIVQGGTDVEFREISSKALVGLGEFDGFAIGGLAVGEPNEEMYATLEYTTPWLPKHKPRYLMGVGTPEDIIEAIDRGVDMFDCVMPTRNARNGTLFTHFGKLSIKSPRYKLDENPIDSECDCYTCKHHSRAYLNHLYRSGEFSYFRLASIHNLRYYLNLVRGAREAILSRTWAEYRRQFYAKRGADEA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Xylella fastidiosa (strain M23)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.373 kDa
Sequence
MSRLQFQLQATDGAARRGQLSFPCGTVQTPTFMPVGTYGAVKGVLPGQLCDLGAEIILGNTFHLFLRPGLEVIADHGGLHGFMRWNGPILTDSGGFQVFSLAHRRKISEQGVTFAAPTDGAQVFLGPEESMKIQKVLNSDVVMIFDECTPYPATEDVARDSMELSLRWAQRSRDAHDALDNDAALFGIIQGGVHPDLRGRSLDGLQAIGFDGYGIGGLAVGESESERNVILEYLHPRLPTDRPRYLMGVGRPEDLVESVARGVDMFDCVMPTRHARNGQYFTGFGTVKIRNACYARDVDPIEQGCGCPACVGGYTRAYLRHLDRCNEMLASMLGSLHNLWYYETLMANMRAAITAGTFFAFRRSFYLARGLDPPPLP

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Xylella fastidiosa (strain Temecula1 / ATCC 700964)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.373 kDa
Sequence
MSRLQFQLQATDGAARRGQLSFPCGTVQTPTFMPVGTYGAVKGVLPGQLCDLGAEIILGNTFHLFLRPGLEVIADHGGLHGFMRWNGPILTDSGGFQVFSLAHRRKISEQGVTFAAPTDGAQVFLGPEESMKIQKVLNSDVVMIFDECTPYPATEDVARDSMELSLRWAQRSRDAHDALDNDAALFGIIQGGVHPDLRGRSLDGLQAIGFDGYGIGGLAVGESESERNVILEYLHPRLPTDRPRYLMGVGRPEDLVESVARGVDMFDCVMPTRHARNGQYFTGFGTVKIRNACYARDVDPIEQGCGCPACVGGYTRAYLRHLDRCNEMLASMLGSLHNLWYYETLMANMRAAITAGTFFAFRRSFYLARGLDPPPLP

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Acinetobacter baumannii (strain AB0057)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.912 kDa
Sequence
MKFEKLGQSGRARRGRLTLEHGVVETPVFMPVGTYGTVKGMLPRDIEDIQAQIILGNTFHLYLRPGLEVIKQHGGLHDFIKWNKPILTDSGGFQVFSLGAMRKIKEEGVTFRSPIDGSKVFLSPEISMEIQHVLNSDIVMIFDECTPYPATHEEAQKSLQLSLRWAKRCKAHHHDELKNKNALFGIIQGGMYEDLRDESLNGLLEIGFDGYAIGGLSVGEPKEEMIKVLDYLPNKMPHDKPRYLMGVGKPEDIVEAVRRGVDMFDCVMPTRNARNGHYFVTDGLVRIRNSKYRHDQGPLDPHCDCYTCKNFTRAYLFHLEKCGEMLASMLGTIHNLRYYQRLTEGMRDALDNGTFDEFVQDFYARRGLEVPPCPVDE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Acinetobacter baumannii (strain ACICU)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.942 kDa
Sequence
MKFEKLGQSGRARRGRLTLEHGVVETPVFMPVGTYGTVKGMLPRDIEDIQAQIILGNTFHLYLRPGLEVIKQHGGLHDFIKWNKPILTDSGGFQVFSLGAMRKIKEEGVTFRSPIDGSKVFLSPEISMEIQHVLNSDIVMIFDECTPYPATHEEAQKSLQLSLRWAKRCKTHHHDELKNKNALFGIIQGGMYEDLRDESLNGLLEIGFDGYAIGGLSVGEPKEEMIKVLDYLPNKMPHDKPRYLMGVGKPEDIVEAVRRGVDMFDCVMPTRNARNGHYFVTDGLVRIRNSKYRHDQGPLDPHCDCYTCKNFTRAYLFHLEKCGEMLASMLGTIHNLRYYQRLTEGMRDALDNGTFDEFVQDFYARRGLEVPPCPVDE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Acinetobacter baumannii (strain SDF)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.94 kDa
Sequence
MKFEKLGQSGRARRGRLTLEHGVVETPIFMPVGTYGTVKGMLPRDIEDIQAQIILGNTFHLYLRPGLEVIKQHGGLHDFIKWNKPILTDSGGFQVFSLGAMRKIKEEGVTFRSPIDGSKVFLSPEISMEIQHVLNSDIVMIFDECTPYPATHEEAQKSLQLSLRWAKRCKAHHHDELKNKNALFGIIQGGMYEDLRDESLNGLLEIGFDGYAIGGLSVGEPKEEMIKVLDYLPNKMPHDKPRYLMGVGKPEDIVEAVRRGVDMFDCVMPTRNARNGHYFVTDGLVRIRNSKYRHDQGPLDPHCDCYTCKNFTRAYLFHLEKCGEMLASMLGTIHNLRYYQRLTEGMRDALDKGTFDEFVQDFYARRGLEVPPCPVDE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.912 kDa
Sequence
MKFEKLGQSGRARRGRLTLEHGVVETPVFMPVGTYGTVKGMLPRDIEDIQAQIILGNTFHLYLRPGLEVIKQHGGLHDFIKWNKPILTDSGGFQVFSLGAMRKIKEEGVTFRSPIDGSKVFLSPEISMEIQHVLNSDIVMIFDECTPYPATHEEAQKSLQLSLRWAKRCKAHHHDELKNKNALFGIIQGGMYEDLRDESLNGLLEIGFDGYAIGGLSVGEPKEEMIKVLDYLPNKMPHDKPRYLMGVGKPEDIVEAVRRGVDMFDCVMPTRNARNGHYFVTDGLVRIRNSKYRHDQGPLDPHCDCYTCKNFTRAYLFHLEKCGEMLASMLGTIHNLRYYQRLTEGMRDALDNGTFDEFVQDFYARRGLEVPPCPVDE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Acinetobacter baumannii (strain AYE)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.912 kDa
Sequence
MKFEKLGQSGRARRGRLTLEHGVVETPVFMPVGTYGTVKGMLPRDIEDIQAQIILGNTFHLYLRPGLEVIKQHGGLHDFIKWNKPILTDSGGFQVFSLGAMRKIKEEGVTFRSPIDGSKVFLSPEISMEIQHVLNSDIVMIFDECTPYPATHEEAQKSLQLSLRWAKRCKAHHHDELKNKNALFGIIQGGMYEDLRDESLNGLLEIGFDGYAIGGLSVGEPKEEMIKVLDYLPNKMPHDKPRYLMGVGKPEDIVEAVRRGVDMFDCVMPTRNARNGHYFVTDGLVRIRNSKYRHDQGPLDPHCDCYTCKNFTRAYLFHLEKCGEMLASMLGTIHNLRYYQRLTEGMRDALDNGTFDEFVQDFYARRGLEVPPCPVDE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.075 kDa
Sequence
MLMSLTLSLQAEDGRARAATLHTAHGDVPTPTFMPVGTAATVKAMMMDSVRATGAGIVLGNTYHLMLRPGADRVAALGGLHRFMDWPGPILTDSGGFQVMSLSSLRKLDKDGVTFQSHIDGSRHRLTPESSIGIQHKLDATITMAFDECTKFPATHEEAASSMELSMRWAARCRDAFVPRDGYGLFGIVQGSVYNDLRTQSVTALGDDFHGYAVGGLAVGEGQEAMFATLDHTLPLLPRGKPRYLMGVGTPDDILGAVMRGVDMFDCVMPTRAGRTARAYTSQGVMNMRNARYADDGRPIDPACDCPACTRHSRAYLHHLFRAGEMLGPMLLTWHNLNYYQSLMRGLRSAIMEGRLEQHAVTLRAAWAAGDREKQDG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.027 kDa
Sequence
MKLKFDLKKKNGNARRGQLTFERGTVQTPAFMPVGTYGTVKGMTPEEVKGTGAEILLGNTFHLWLRPGQEVMKMHGDLHDFMNWHGPILTDSGGFQVFSLGKMRTITEKGVHFRNPVNGDKIFMDAEKSMEIQKDLGSDIVMIFDECTPYPATHNEAKKSMEMSLRWAQRSRDHFDKLENPNNLFGIVQGGVYEDLRDVSVKGLTEIGFDGYAVGGLAVGEPKEDMHRILEHTCPQLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGVIKIRNAKHKTDTTPLDPHCDCYTCQNYSKSYLHHLERCNEILGARLNTIHNLRYYQRLMESIRKAIDEDRFDEFVQEFYARRDREVPPLSKA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.704 kDa
Sequence
MKFELDTTQGRARRGRLIFDRGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQDSLGSDVVMIFDECTPYPATEDEARKSMQMSLRWAQRSRDEFDRLENPNALFGIIQGGVYEDLRDESLTGLVNIGFDGYAIGGLAVGEPKPDMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTAPLDEKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVSDFYTGLGREVPEVPELVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella halifaxensis (strain HAW-EB4)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.869 kDa
Sequence
MKFELDTTQGRARRGRLIFERGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQDSLGSDVVMIFDECTPYPATEDEARKSMQMSLRWAQRSRDEFDRLENPNSLFGIIQGGVYEDLRDESLNGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPKIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDDKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQRLMEGLRGAIETGTLDAFVTEFYTSQGREVPEVPELTD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella pealeana (strain ATCC 700345 / ANG-SQ1)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.913 kDa
Sequence
MKFELDTTQGRARRGRLIFERGTVETPAFMPVGTYGTVKGMTPEEVRETGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQDSLGSDVVMIFDECTPYPATEDEARKSMQMSLRWAQRSRDEFDRLENPNSLFGIIQGGVYEDLRDESLNGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPKIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDDKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQRLMEGLRGAIETGTLDAFVTEFYTSQGREVPEVPELSD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella piezotolerans (strain WP3 / JCM 13877)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.904 kDa
Sequence
MKFELDTTQGRARRGRLVFERGTVETPAFMPVGTYGTVKGMTPEEVRETGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQDSLGSDVVMIFDECTPYPATEDEARKSMQMSLRWAQRSRDEFDRLENPNSLFGIIQGGVYEGLRDESLKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHTCPQIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVVKIRNARHRDDTSTLDDKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQRLMEGLRGAIETGTLDDFVTEFYTSQGREVPEVPELTD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella sediminis (strain HAW-EB3)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.827 kDa
Sequence
MKFELDTTQGRARRGRLVFERGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQNSLGSDVVMIFDECTPYPATEDEARKSMQMSLRWAQRSRDEFDKLENPNSLFGIIQGGVYEDLRDESLKGLVDIGFDGYAVGGLAVGEPKADMHRILEHTCPQIPTDKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTTEGVIKIRNARHRDDTSPLDDKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQKLMEGLRGAIETGTLDAFVEEFYTSQGREVPEVPELTD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Desulfovibrio alaskensis (strain G20)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.733 kDa
Sequence
MATIGEFTLHATDGKARTGVLQTAHGPVRTPIFMPVGTVGSVKGVAPDDLDAIGAEIILGNTYHLYLRPGDELVARRGGLHEFNAWRKPILTDSGGFQVFSLSGLRRISEEGVEFRSHLDGSKHLFTPEKVVSIQRNLNSDIMMVLDECVPYGADKDYTARSLKMTTRWAQRCRDAYPAGSGGNLMFGITQGGFFKDLREESIGELTRIDFDGFALGGLSVGESKTEMMDILYHTAPMLPAHKPRYLMGVGTPLDIINGINAGIDMFDCVLPTRNARNGTLYTSAGKINIKRREFAEDDGPLDPNCSCYTCRTFSRAYLRHLFHAQEILSYRLNSIHNLTYFLDLVRGAREAIAQGTFAEYKSRYDAIYPQEAALCP

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Acinetobacter baumannii (strain AB307-0294)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.912 kDa
Sequence
MKFEKLGQSGRARRGRLTLEHGVVETPVFMPVGTYGTVKGMLPRDIEDIQAQIILGNTFHLYLRPGLEVIKQHGGLHDFIKWNKPILTDSGGFQVFSLGAMRKIKEEGVTFRSPIDGSKVFLSPEISMEIQHVLNSDIVMIFDECTPYPATHEEAQKSLQLSLRWAKRCKAHHHDELKNKNALFGIIQGGMYEDLRDESLNGLLEIGFDGYAIGGLSVGEPKEEMIKVLDYLPNKMPHDKPRYLMGVGKPEDIVEAVRRGVDMFDCVMPTRNARNGHYFVTDGLVRIRNSKYRHDQGPLDPHCDCYTCKNFTRAYLFHLEKCGEMLASMLGTIHNLRYYQRLTEGMRDALDNGTFDEFVQDFYARRGLEVPPCPVDE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Brucella suis biovar 1 (strain 1330)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.452 kDa
Sequence
MTTENFGFKVLARDGAARQGEISMPRGVVRTPAFMPVGTAGTVKAMYMDQVKELGADIILGNTYHLMLRPGAERVARLGGLHEFGGWKGPILTDSGGFQVMSLAQLRKLNEHGVTFRSHIDGKAYEMTPERSIEIQGLLDSDIQMQLDECVALPSPEKNTERAMELSLRWAERCKVAFGDQPGKAMFGIVQGGDIARLRERSAEALKAMDLKGYSVGGLAVGEPQEVMLDMLEVVCPILPTEKPRYLMGVGTPDDILKSVARGIDMFDCVMPTRAGRHGLAFTRFGKVNLRNARHAEDHRPLDPQSDCPASRDYSRAYLHHLVKSGEALGAMLLTWNNLAYYQYLMKGIRAAIADGNFSDFTAETTEGWARGDMPAL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Length
377 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.466 kDa
Sequence
MTTENFGFKVLARDGAARQGEISMPRGVVRTPAFMPVGTAGTVKAMYMDQVKELGADIILGNTYHLMLRPGAERVARLGGLHEFGGWKGPILTDSGGFQVMSLAQLRKLNEHGVTFRSHIDGKAYEMTPERSIEIQGLLDSDIQMQLDECVALPSPEKNTERAMELSLRWAERCKVAFGDQPGKAMFGIVQGGDIARLRERSAEALKAMDLKGYSVGGLAVGEPQEVMLDMLEVVCPILPTEKPRYLMGVGTPDDILKSVARGIDMFDCVMPTRAGRHGLAFTRFGKVNLRNARHAEDHRPLDPQSDCPASRDYSRAYLHHLVKSGEALGAMLLTWNNLAYYQYLMKGIRAAIADGKFSDFTAETTEGWARGDMPAL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Agrobacterium fabrum (strain C58 / ATCC 33970)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.945 kDa
Sequence
MHEKFTFTLKSTSGGARLGEVAMPRGVIRTPAFMPVGTVGTVKAMYLDQVRELGADIILGNTYHLMLRPGPERVARLGGLHELIRWPHPILTDSGGFQVMSLSGLRKLDEKGVTFKSHVDGSLHHMSPERSIEIQGMLDSDIQMQLDECIALPAERKEIERAMEMSLRWAERCRVAFGEQPGKAMFGIVQGGDQPDLRIRSAEGLKELDLKGYAVGGLAVGEPQDVMLGMLDITLPVLPTEKPRYLMGVGTPDDILKSVARGIDMFDCVMPTRSGRHGLAFTRRGRVNIRNARHAEDMRPLDEQSNCPASRDYSRAYLHHLTRSNEALGGMLLSWHNLAYYQELMQGIRTSIEEGRFADFYAETIEMWARGDIDPV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.714 kDa
Sequence
MYTLLKKTGKVRRGRFETVHGTIETPVFMNVGTLAAIKGAVSSMDLKEINCQVELSNTYHLSLRPGDDVVKKLGGLHKFMNWDRPILTDSGGFQVFSLAEIRKIKEEGVYFNSHIDGRKIFMGPEESMKIQSNLASTIAMAFDECVENPSPREYVERSVERTTRWLVRCKEELDRLNSLPDTINKKQMLFGINQGGVYDDIRIEHAKTIAKMDLDGYAIGGLAVGETHEEMYRIIDAVVPHLPQDKPIYLMGVGTPSNILEAVSRGVDFFDCVLPARNGRHGHVFTKHGKINLRNEKFELDASPIDEGCQCPTCKHYSRAYIRHLFKAKEMLAMRLCVLHNLYFYNTLMEDIRNAIDADCFEEFKNEKLKAWAGKA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium botulinum (strain ATCC 19397 / Type A)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.939 kDa
Sequence
MYKLLKKSGKARRGEFTTPHGVIQTPVFMNVGTLAAIKGAVSSMDLKEIGCQVELSNTYHLHLRPGDEVVKKMGGLHKFMNWDRPILTDSGGFQVFSLSKIRKIQEEGVYFNSHIDGRKIFMGPEESMRIQSNLASTIAMAFDECVENPAPREYVEKSVERTTRWLHRCKDEMNRLNSLPDTINNKQMLFGINQGGTYEDIRIEHAKTIAKMDLDGYAIGGLAVGESHEDMYRIIDAVVPHLPEDKPIYLMGVGIPSNILEAVDRGVDFFDCVLPARNGRHAHVFTKEGKINLLNAKFELDDRPIDEGCQCPACKHYTRSYIRHLFKAKEMLAMRLCVLHNLYFYNNLMEEIRDAIDGNYFKEYKERKLKEWGGRA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium botulinum (strain 657 / Type Ba4)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.94 kDa
Sequence
MYKLLKKSGKARRGEFTTPHGVIQTPVFMNVGTLAAIKGAVSSMDLKEIGCQVELSNTYHLHLRPGDEVVKKMGGLHKFMNWDRPILTDSGGFQVFSLSKIRKIQEEGVYFNSHIDGRKIFMGPEESMRIQSNLASTIAMAFDECVENPAPREYVEKSVERTTRWLHRCKDEMNRLNSLPDTINNKQMLFGINQGGTYEDIRIEHAKTIAKMDLDGYAIGGLAVGESHEDMYRIIDAVVPHLPEDKPIYLMGVGIPSNILEAVDRGVDFFDCVLPARNGRHAHVFTKEGKINLLNAKFELDDRPIDEGCQCPACKHYTRSYIRHLFKAKEMLAMRLCVLHNLYFYNNLMEEIRDAIDGDYFKEYKERKLKEWGGRA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.939 kDa
Sequence
MYKLLKKSGKARRGEFTTPHGVIQTPVFMNVGTLAAIKGAVSSMDLKEIGCQVELSNTYHLHLRPGDEVVKKMGGLHKFMNWDRPILTDSGGFQVFSLSKIRKIQEEGVYFNSHIDGRKIFMGPEESMRIQSNLASTIAMAFDECVENPAPREYVEKSVERTTRWLHRCKDEMNRLNSLPDTINNKQMLFGINQGGTYEDIRIEHAKTIAKMDLDGYAIGGLAVGESHEDMYRIIDAVVPHLPEDKPIYLMGVGIPSNILEAVDRGVDFFDCVLPARNGRHAHVFTKEGKINLLNAKFELDDRPIDEGCQCPACKHYTRSYIRHLFKAKEMLAMRLCVLHNLYFYNNLMEEIRDAIDGNYFKEYKERKLKEWGGRA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium botulinum (strain Kyoto / Type A2)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.94 kDa
Sequence
MYKLLKKSGKARRGEFTTPHGVIQTPVFMNVGTLAAIKGAVSSMDLKEIGCQVELSNTYHLHLRPGDEVVKKMGGLHKFMNWDRPILTDSGGFQVFSLSKIRKIQEEGVYFNSHIDGRKIFMGPEESMRIQSNLASTIAMAFDECVENPAPREYVEKSVERTTRWLHRCKDEMNRLNSLPDTINNKQMLFGINQGGTYEDIRIEHAKTIAKMDLDGYAIGGLAVGESHEDMYRIIDAVVPHLPEDKPIYLMGVGIPSNILEAVDRGVDFFDCVLPARNGRHAHVFTKEGKINLLNAKFELDDRPIDEGCQCPACKHYTRSYIRHLFKAKEMLAMRLCVLHNLYFYNNLMEEIRDAIDGDYFKEYKERKLKEWGGRA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium botulinum (strain Okra / Type B1)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.912 kDa
Sequence
MYKLLKKSGKARRGEFTTPHGVIQTPVFMNVGTLAAIKGAVSSMDLKEIGCQVELSNTYHLHLRPGDEVVKKMGGLHKFMNWDRPILTDSGGFQVFSLSKIRKIQEEGVYFNSHIDGRKIFMGPEESMRIQSNLASTIAMAFDECVENPAPREYVEKSVERTTRWLHRCKDEMNRLNSLPDTINNKQMLFGINQGGTYEDIRIEHAKTIAKMDLDGYAIGGLAVGESHEDMYRIIDAVVPHLPEDKPIYLMGVGIPSNILEAVDRGVDFFDCVLPARNGRHAHVFTKEGKINLLNAKFELDDKPIDEGCQCPACKHYTRSYIRHLFKAKEMLAMRLCVLHNLYFYNNLMEEIRDAIDGDYFKEYKERKLKEWGGRA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium botulinum (strain Langeland / NCTC 10281 / Type F)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.912 kDa
Sequence
MYKLLKKSGKARRGEFTTPHGVIQTPVFMNVGTLAAIKGAVSSMDLKEIGCQVELSNTYHLHLRPGDEVVKKMGGLHKFMNWDRPILTDSGGFQVFSLSKIRKIQEEGVYFNSHIDGRKIFMGPEESMRIQSNLASTIAMAFDECVENPAPREYVEKSVERTTRWLHRCKDEMNRLNSLPDTINNKQMLFGINQGGTYEDIRIEHAKTIAKMDLDGYAIGGLAVGESHEDMYRIIDAVVPHLPEDKPIYLMGVGIPSNILEAVDRGVDFFDCVLPARNGRHAHVFTKEGKINLLNAKFELDDKPIDEGCQCPACKHYTRSYIRHLFKAKEMLAMRLCVLHNLYFYNNLMEEIRDAIDGDYFKEYKERKLKEWGGRA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium botulinum (strain Loch Maree / Type A3)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.94 kDa
Sequence
MYKLLKKSGKARRGEFTTPHGVIQTPVFMNVGTLAAIKGAVSSMDLKEIGCQVELSNTYHLHLRPGDEVVKKMGGLHKFMNWDRPILTDSGGFQVFSLSKIRKIQEEGVYFNSHIDGRKIFMGPEESMRIQSNLASTIAMAFDECVENPAPREYVEKSVERTTRWLHRCKDEMNRLNSLPDTINNKQMLFGINQGGTYEDIRIEHAKTIAKMDLDGYAIGGLAVGESHEDMYRIIDAVVPHLPEDKPIYLMGVGIPSNILEAVDRGVDFFDCVLPARNGRHAHVFTKEGKINLLNAKFELDDRPIDEGCQCPACKHYTRSYIRHLFKAKEMLAMRLCVLHNLYFYNNLMEEIRDAIDGDYFKEYKERKLKEWGGRA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.49 kDa
Sequence
MAKPFSFKVLATDGRARRGIIDMPRGEIRTPAFMPVGTGGTVKTMYMDQVRGVGADIILGNTYHLMLRPGAERVARLGGLHEFARWPHPILTDSGGFQVMSLSKLRKLTEKGVTFRSHIDGAPYEMSPERSIEIQSLLDSDIQMQLDECTALPAELKEIERAMELSLRWAERCKTAFGDQPGKAMFGIVQGGDNAALRVRSAQALSAMGLKGYAVGGLAVGEPQAVMLEMLDITCPELPADKPRYLMGVGTPDDILKSVARGIDMFDCVMPTRAGRHGLAYTRRGKVNLRNARHADDPRPLDEESDCPAARDYSRAYLHHLVRSQEALGAMLLTWNNLSYYQKLMQDIRAAIETQTFEARGAEITEGWARGDIPVL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rhizobium meliloti (strain 1021)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.797 kDa
Sequence
MTETFQFKLLAADGNARRGEVVTPRGTIRTPAFMPVGTVGTVKAMYLDQVRDLGADIILGNTYHLMLRPGAERVARLGGLHKFIRWERPILTDSGGFQVMSLSSLRKLNEQGVTFKSHVDGALYHMSPERSIEIQGLLGSDIQMQLDECVALPAEPDEIERAMEMSLRWAERCKVAFGDQPGKAMFGIVQGGDIPRLRERSALALRDLDLKGYAVGGLAVGEPQEVMLGMLDVTCPVLPADKPRYLMGVGTPDDILKSVAHGIDMFDCVMPTRSGRHGLAFTRYGRINLRNARHAEDTRPLDEQSSCPATRDYSRAYLHHLIRSNESLGGMLLSWNNLAYYQELMAGIRKAIEEGRYTDFMAETMEGWQRGDLPPV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.514 kDa
Sequence
MTQRFSFELTATDGRARTGVISTPRGEIRTPAFMPVGTAGTVKAMLPENVRATGADILLGNTYHLMLRPTAERVARLGGLHRFMNWDRPILTDSGGFQVMSLADLRKLSEEGVTFRSHIDGSKHHLSPERSMEIQRLLGSDIVMAFDECPALPATEEAVAQSMRLSMRWARRSREAFGDRPGHALFGIMQGGVTRDLREESAAALREIGFEGYAIGGLAVGEGQEAMFGVLDYAPGFLPEDRPRYLMGVGKPDDIVGAVERGVDMMDCVLPSRSGRTGQAWTRRGQVNIKNARHMDDPRPLDEACSCPACRSYSRAYLHHVFRAQEIIASMLLTWHNLHYYQELMQGLRTAIAAGRLGEFVAAFHAARAEGDIEPL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.508 kDa
Sequence
MTQRFSFELTATDGRARTGVISTPRGEIRTPAFMPVGTAGTVKAMLPENVRATGADILLGNTYHLMLRPTAERVVRLGGLHRFMNWDRPILTDSGGFQVMSLADLRKLSEEGVTFRSHIDGSKHHLSPERSMEIQRLLGSDIVMAFDECPALPATEEAVAQSMRLSMRWARRSREAFGDRPGHALFGIMQGGVTRDLREESAAALREIGFEGYAIGGLAVGEGQEAMFGVLDYAPGLLPEDRPRYLMGVGKPDDIVGAVERGVDMMDCVLPSRSGRTGQAWTRRGQVNIKNARHMDDPRPLDEACSCPACRSYSRAYLHHVFRAQEIIASMLLTWHNLHYYQELMQGLRTAIAAGRLGEFVAAFHAARAEGDIEPL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Haemophilus somnus (strain 129Pt)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.081 kDa
Sequence
MKFTLHKTNGMARRGTMTFNRPQGEFTVETPAFMPVGTYGTVKGMTPEEVRVTGAEILLGNTFHLWLRPGQEIMRQHGDLHDFMQWHRPILTDSGGFQVFSLGKLRKITEEGVKFQNPINGERIFLSPEKSMEIQYDLGSDIVMIFDECTPYPATFDYAKKSMEMSLRWAKRSRERFDELGNKNALFGIVQGSTFEDLRKLSIEGLINIGFDGYAVGGLAVGEPKEDMHRILAYVCPQLPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVSNGIVKIRNAKYRNDTTSLDPECDCYTCKHYTKAYLYHLDKCGEILGARLNTIHNLHYYQRLMAQIRQAIEEDRFEDFVVEFYKKIGKSVPTR

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Jannaschia sp. (strain CCS1)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.389 kDa
Sequence
MTRASSFRLDATSGKARTGVIQTPRGDIRTPAFMPVGTAATVKAMMPESVAATGADILLGNTYHLMLRPTAERIANLGGLHSFMNWDKPILTDSGGFQVMSLADLRKLTEEGVTFRSHIDGSKHLLSPERSMEIQKLLGSDIVMCFDECPALPADRKALDDSMRLSMRWAARSKEAFGDRPGYALFGIQQGGLEEDLREESAKALREIGFDGYAVGGLAVGEGQAAMFGCLDFAPDQLPTDKPRYLMGVGKPDDIVGAVKRGIDMMDCVLPSRSGRTGQAWTRRGQVNIKNARHADDPRPLDEDCTCPACRNYSRAYLHHVFRAQEMISGMLLTWHNLHYYQELMQTMRDAIAANDFAGFEARFHADRAEGDIVPL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.607 kDa
Sequence
MTQRFSFTRLGQDGAARLGRINTPRGEIRTPAFMPVGTAATVKAMRPESVRETGADILLGNTYHLMLRPTAERIARLGGLHRFMNWDRPILTDSGGFQVMSLTGLRKLTEQGVTFKSHIDGSKHMLSPERSMEIQKLLRSDIVMCFDECPALPAPRERITESMELSMRWAARSREAFGDWPGHALFGIQQGGLEEDLRGKSAEALRAIEFDGYAVGGLAVGEGQEAMFGVLDYAPGMLPEDKPRYLMGVGKPGDLVGAVKRGIDMFDCVLPSRSGRTGQVFTRRGVVNIKNARHADDPRPLDEDCTCPACRSYSRAYLHHVFRAGEILSSMLLTWHNLHYYQELMQGMRDAIGAGDFAGFEARFLAQQAEGDIAPV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Stenotrophomonas maltophilia (strain R551-3)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.51 kDa
Sequence
MSRLQFQLQTRDGRARRGRLTFPRGTVETPAFMPVGTYGSVKGILPDQVRALGAEIILGNTFHLYLRPGLDIIADHGGLHGFCRWDGPILTDSGGFQVFSLAHRRKITEQGVTFASPTDGARVFLGPEESMKIQKVLDSDVVMIFDECTPYPATEDVARRSMELSLRWAQRSRNAHDELGNDAALFGIVQGGVHTDLRSRSADALQAIGFDGYAIGGLAVGEPEDERNAMLDHLDPELPADRPRYLMGVGRPEDLVEGVARGVDMFDCVMPTRNARNGHYFTSFGTVRIRNSQYARDMDPIEPGCGCVACTGGYTRSYLRHLDRCNEMLAPMLGTLHNLFYYEKLMADIRAAIEAGTFLAFRESFYAARGAVAPPL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Stenotrophomonas maltophilia (strain K279a)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.535 kDa
Sequence
MSRLQFQLQTRDGRARRGRLTFPRGTVETPAFMPVGTYGSVKGILPDDVRALGAEIILGNTFHLYLRPGLDIIADHGGLHGFCRWDGPILTDSGGFQVFSLAHRRKITEQGVTFASPTDGARVFLGPEESMKIQKVLDSDVVMIFDECTPYPATEDVARRSMELSLRWAQRSRNAHDELGNDAALFGIVQGGVHTDLRSRSAEALQAIGFDGYAVGGLAVGEPEHERNAMLDHLDPELPSDRPRYLMGVGRPEDLVEGVARGVDMFDCVMPTRNARNGHYFTSFGTVRIRNSQYARDMDPIEPGCGCVACTGGYTRSYLRHLDRCNEMLAPMLGTLHNLFYYEKLMADIRAAIEAGTFLAFRESFYAARGAVAPPL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Erwinia tasmaniensis (strain DSM 17950 / CIP 109463 / Et1/99)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.69 kDa
Sequence
MKFELDTTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVQDTGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEKGVHFRNPINGDAIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAQRSRDRFDSLGNKNALFGIIQGSVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQLPQDKPRYLMGVGKPQDLVEGVRRGVDMFDCVMPTRNARNGHLFVSDGVVKIRNAKYKDDISPLDAECDCYTCRNYSRAYLYHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLEHFVSEFYQRTGAAVPPITSDN

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium kluyveri (strain NBRC 12016)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.898 kDa
Sequence
MYKLLKKDGSSRRGEFSTPHGVVQTPVFMNVGTLAAIKGAVSTEDLKEIGCQIELSNTYHLSLRPGDEVIRKLGGLHKFMNWDRPILTDSGGFQVFSLSGMRKIKEEGVYFNSHIDGRKIFMGPEESMRIQSNLASTVAMAFDECVENPAPKEYVEDSVKRTTRWLKRCKIEIDRLNSMPHTINNKQMLFGINQGGVHDDIRMEHAKIISDMDLDGYAIGGLAVGETHEEMYRVLEKVVPNLPENKPIYLMGVGTPANILEAVERGVDFFDCVMPSRNGRHSHVFTSYGVIHLLNAKYELDDNPIDSECSCPTCKNYTRAYIRHLFKAKEMLAMRLCVIHNLYFYNNLMKEIRESIDKGNFLQYKKEKLEKWNETV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.898 kDa
Sequence
MYKLLKKDGSSRRGEFSTPHGVVQTPVFMNVGTLAAIKGAVSTEDLKEIGCQIELSNTYHLSLRPGDEVIRKLGGLHKFMNWDRPILTDSGGFQVFSLSGMRKIKEEGVYFNSHIDGRKIFMGPEESMRIQSNLASTVAMAFDECVENPAPKEYVEDSVKRTTRWLKRCKIEIDRLNSMPHTINNKQMLFGINQGGVHDDIRMEHAKIISDMDLDGYAIGGLAVGETHEEMYRVLEKVVPNLPENKPIYLMGVGTPANILEAVERGVDFFDCVMPSRNGRHSHVFTSYGVIHLLNAKYELDDNPIDSECSCPTCKNYTRAYIRHLFKAKEMLAMRLCVIHNLYFYNNLMKEIRESIDKGNFLQYKKEKLEKWNETV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium tetani (strain Massachusetts / E88)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.835 kDa
Sequence
MYTLIKKCGNAKRGRFETPHGTIETPVFMNVGTLGVIKGAVSSMDLKEIGCQVELSNTYHLHLRPGDEVIKKMGGLHKFMNWDRPILTDSGGFQVFSLAKIRKIQEEGVYFNSHIDGRRIFMGPEESMRIQSNIASTIAMAFDECIPNPSTREYVENSVARTTRWLERCKKEMDRLNSLPDTINKKQMLFGINQGGTYEDIRKAHAKTIVDMDLDGYAIGGLAVGETHEEMYRVIDEVAPIFPDNKPLYLMGVGLPSNILEAVDRGVDFFDCVLPARNGRHGHVFTKYGKINLMNAKFELDGNPIDEGCECPACKHYSRAYIRHLFKAKEMLAMRLCVLHNLYFYNKLMEDIRKAIEGDYFKEFKEEKLHNWSGKA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.535 kDa
Sequence
MLNFELLTTDGNARRGRVTLNHGVVETPIFMPVGTYGSVKAMSPLELNEIGAQIILGNTFHLWLRPGLDVVDTHAGLHKFIGWDKPILTDSGGFQVFSLGELRKITEEGVTFASPVNGDKLFLSPEISMQIQRTLNSDIVMQFDECTPYEIDGRPATHDEAARSMRMSLRWAKRSRDEFDHLANPNALFGIVQGGMFEDLRDESLAGLSELDFHGYAIGGLSVGEPKEDMMRVLEHVGPRLPAHKPHYLMGVGTPEDLVAGVAHGVDMFDCVMPTRNARNGWLFTRFGDVKIRNAAHRNDPRPLDEQCGCYTCRNFSRAYLHHLHRVGEILGARLNTIHNLYYYLELMREMRTAIEEHRFEAFRRQFAENRARGTR

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.339 kDa
Sequence
MLNFELITTDGNARRGRVTLNHGVVETPIFMPVGTYGSVKAMSPLELNEIGAHIILGNTFHLWLRPGLDVVNAHEGLHKFIGWDKPILTDSGGFQVFSLGDLRKITEDGVTFASPVNGDKLFLSPEISMQIQRTLNSDIVMQFDECTPYEIDGRAATHEEAAKSMRMSLRWAKRSRDEFERLANPNALFGIVQGGMYEDLRDESLAGLSELDFHGFAIGGLSVGEPKEDMMRVLEHVAPRLPAHKPHYLMGVGTPEDLVAGVAAGVDMFDCVMPTRNARNGWLFTRFGDVKIKNAAHRNDPRPLDESCACYTCRNFSRAYLHHLHRVGEILGARLNTIHNLHYYLQLMREMREAIEHHRFADFRRQFAADRARGTQ

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Cupriavidus necator (strain JMP 134 / LMG 1197)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.47 kDa
Sequence
MLNFELITTDGNARRGRVTLNHGVVETPIFMPVGTYGSVKAMSPLELNEIGAEIILGNTFHLWLRPGLDVVNTHEGLHRFIGWDKPILTDSGGFQVFSLGDLRKITEDGVTFASPVNGDKLFLSPEISMQIQRTLNSDIVMQFDECTPYEIEGRPATHEEAAKSMRMSLRWAKRSRDEFERLANPNALFGIVQGGMFEDLRDESLAGLSELDFHGFAIGGLSVGEPKEDMMRVLEHVAPRLPADKPHYLMGVGTPEDLVAGVAAGVDMFDCVMPTRNARNGWLFTRYGDVKIRNAAHRNDPRPLDESCACYTCRNFSRAYLHHLHRVGEILGARLNTIHNLHYYLQLMREVRESIEQHRFSDFRRQFASDRARGTR

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.364 kDa
Sequence
MLNFELITTDGNARRGRVTLNHGVVETPIFMPVGTYGSVKAMSPLELNEIGAQIILGNTFHLWLRPGLDVVNAHEGLHRFIGWDKPILTDSGGFQVFSLGDLRKITEDGVTFASPVNGDKLFLSPEISMQIQRTLNSDIVMQFDECTPYEIDGRPATHEEAAKSMRMSLRWARRSRDEFERLANPNALFGIVQGGMYEDLRDESLAGLSELDFHGFAIGGLSVGEPKEDMMRVLEHVAPRLPANKPHYLMGVGTPEDLVAGVAAGVDMFDCVMPTRNARNGWLFTRYGDVKIKNAAHRNDPRPLDESCACYTCRNFSRAYLHHLHRVGEILGARLNTIHNLHYYLQLMREVREAIEQHRFADFRRQFAADRARGTQ

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.641 kDa
Sequence
MSERFSFDLHASDGKARTGVIHTPRGGVRTPAFMPVGTAATVKAMMPESVRATGADILLGNTYHLMLRPTAERIDRLGGLHRFMNWDRPILTDSGGFQVMSLAGLRKLTEKGVTFKSHIDGSKHELTPERSMEIQRLLGSDIVMCFDECPALPADRDRIAESMRLSMRWAERSREAFGDRPGHALFGIMQGGLEQDLREESAQALRSVGFDGYAVGGLAVGEGQAAMFDCLDYAPGFLPEDKPRYLMGVGKPDDIVGAVKRGIDMMDCVLPSRSGRTGQVFTRHGVLNIKNARHMDDPRPLDEACTCPACRNYSRAYLHHVFRSQEIISSMLLTWHNLHYFQEIMQGMREAIAGGTFEAWEAAFHAGRAQGDIEPL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Ruegeria sp. (strain TM1040)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.744 kDa
Sequence
MAELFNFEMTATDGKARTGVIHTPRGEIRTPAFMPVGTAATVKAMMPESVRATGADILLGNTYHLMLRPTAERIDRLGGLHKFMNWDRPILTDSGGFQVMSLAGLRKLTEKGVTFKSHIDGSRHELTPERSMEIQRLLGSDIVMCFDECPALPADRDRIAESMRLSMRWAERSREAFGDRPGHALFGIQQGGLEQDFREESAEALTKIGFDGYAVGGLAVGEGQEAMFGCLDYAPDMLPVDKPRYLMGVGKPDDIVGAVSRGIDMMDCVLPSRSGRTGQAFTRHGVVNIKNARHQDDPRPLDENCSCPACSNYSRAYLHHVFRSNEMISGMLLTWHNLHYFQDIMAGMRESIAAGTFEAWQKTFHETRAQGDIEPL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Campylobacter concisus (strain 13826)
Length
376 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.535 kDa
Sequence
MKFEVIKKDGNARRGILTTAHSVIQTPVFMPVGTVGAVKSLDAFDMSEILDAKIILANTYHMYLRPGSKVVREFGGLHGFSKFDRSFLTDSGGFQAFSLRSNTKNDDGGIKFKSHIDGSTHYFTPRSVLDTQYELGSDIMMILDDLVALPAEPKRIDLSIKRTIKWAKEAIDYHKFMQSKGVGLQQNIFGIVQGGTDYEARKFCAEALNEMPFDGLAIGGLSVGESNEAMYDTVEAVMPFMDELRPRYLMGVGTPEDLVENVERGVDMFDCVMPTRNARNGTLFTSFGKINIKSAKFINDHAPIDPQCQCYTCKRYSRGYLNHLFKARELTFFRLASLHNLHYYLNLMKEMREAIEVGEFAKFKRNFYAKRSTDEL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Photobacterium profundum (strain SS9)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.741 kDa
Sequence
MKFELDKTQGRARRGRLQFERGTVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEVMKLHGDLHDFMQWHGPILTDSGGFQVFSLGATRKITEEGVHFRNPVNGDKVFMDAEKSMEIQYDLGSDIVMIFDECTPYPATHDEAKKSMEMSLRWAQRSRNHFDKQENPNALFGIIQGGVYEDLRDVSVDGLTNIGFDGYAVGGLAVGEPKEDMHRILEHTCPQLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGVIKIRNAKHKTDTTPLDPHCDCYTCLNYSKAYLYHLDKCNEILGSRLNTIHNLRYYQRLMASIRSAIEEDRFDVFVEEFYARRDREVPPLKNA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Aliivibrio fischeri (strain ATCC 700601 / ES114)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.912 kDa
Sequence
MKYELIKKQGRARRGQLQFDRGTVETPAFMPVGTYGTVKGMTPEEVKGTGAEILLGNTFHLWLRPGQEIMKLHGDLHDFMNWKGPILTDSGGFQVFSLGKTRKITEEGVHFRSPVNGDKIFMDAEKSMQIQYDLGSDVVMIFDECTPYPATHDEARISMERSIRWAERSRNEFDRQENPNALFGIVQGGVYEDLRDVSVEALTKIGFDGYAVGGLAVGEPKEDMHRILEHTCPQLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGVIKIRNAKHKTDTTPLDPECDCYTCQNYSKSYLHHLDRCNEILGARLNTIHNLRYYQRIMASIRKALEEDRFEQFVEEFYARRDREVPPLKDL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Aliivibrio fischeri (strain MJ11)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.912 kDa
Sequence
MKYELIKKQGRARRGQLQFDRGTVETPAFMPVGTYGTVKGMTPEEVKGTGAEILLGNTFHLWLRPGQEIMKLHGDLHDFMNWKGPILTDSGGFQVFSLGKTRKITEEGVHFRSPVNGDKIFMDAEKSMQIQYDLGSDVVMIFDECTPYPATHDEARISMERSIRWAERSRNEFDRQENPNALFGIVQGGVYEDLRDVSVEALTKIGFDGYAVGGLAVGEPKEDMHRILEHTCPQLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGVIKIRNAKHKTDTTPLDPECDCYTCQNYSKSYLHHLDRCNEILGARLNTIHNLRYYQRIMASIRKALEEDRFEQFVEEFYARRDREVPPLKDL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Aliivibrio salmonicida (strain LFI1238)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.939 kDa
Sequence
MKYELIKKQGRARRGQLQFDRGTVETPAFMPVGTYGTVKGMTPEEVKDTGAEILLGNTFHLWLRPGQEIMKLHGDLHDFMNWKGPILTDSGGFQVFSLGKTRKITEEGVHFRSPVNGDKIFMDAEKSMQIQYDLGSDVVMIFDECTPYPATHDEARISMERSIRWADRSRNEFDRQENPNALFGIVQGGVYEDLRDVSVEALTKIGFDGYAVGGLAVGEPKEDMHRILEHTCPLLPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTGGIVKIRNAKHKVDTTPLDPECDCYTCQNYSKSYLHHLDRCNEILGARLNTIHNLRYYQRIMASIRKALEEDRFEQFVEEFYARRDREVPPLKDL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.536 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDGLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shigella boydii serotype 4 (strain Sb227)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shigella dysenteriae serotype 1 (strain Sd197)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shigella flexneri serotype 5b (strain 8401)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.608 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSIYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shigella flexneri
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.608 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSIYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shigella sonnei (strain Ss046)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.786 kDa
Sequence
MKPRFAFSISATDGAARAGVIAMQRGEIRTPAFMPVGTAATVKAMRPAEVRAAGADIILGNTYHLMLRPTAERMARFGGLHKFMGWDRPILTDSGGYQVMSLSALTKQSEEGVAFKSHLDGSRHMLTPERSMEIQRLLGSDIVMAFDECPPAGVDARRAEASMERSMRWAARSRAGFDAGEEHAARSALFGIQQGSLDEKLRARSAATLIDIGFDGYAIGGLAVGEGQAAMFGVLDFAPAQLPADRPRYLMGVGKPDDLVGAVARGVDMFDCVLPTRSGRNGQAFTWDGPLNIRNAKFADDQEPLDASCGCPVCTIWSRGYLHHLVRAGEMLGAMLMTQHNIHFYQDLMQAMRDAITTGRFAAFRSDFAARYRRA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Herminiimonas arsenicoxydans
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.223 kDa
Sequence
MLNFKLLNTDGNARRGQLTVNHGVIETPIFMPVGTYGSVKAMSPLELKEIDAQIILGNTFHLWLRPGNDIVAKFGGLHEFMGWDKPILTDSGGFQVFSLGEMRKITEEGVHFSSPINGDKLFLSPEVSMQIQRVLNSDIVMQFDECTPYEIDGRPATADEAAKSMRMSLRWAKRSIDEFNREENPNALFGIVQGGMFEHLRDESLAGLEDINFHGVAIGGLSVGEPKEDMLRVLQHVGPRLPANKPHYLMGVGTPEDLVQGVANGIDMFDCVMPTRNARNGWLFTRFGDIKIKNARYKDDKKPLDASCGCYACRNFSRAYLHHLHRTGEILGARLNTIHNLHYYLDLMREMREAISEGRFQLFVKQFHADRARGA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Janthinobacterium sp. (strain Marseille)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.301 kDa
Sequence
MLNFKLLKTDGNARRGQLTLNHGVIETPIFMPVGTYGSVKAMSPLELNEIDAQIILGNTFHLWLRPGNDIIAKFGGLHEFMGWNKPILTDSGGFQVFSLGEMRKITEEGVHFSSPINGDKLFLSPEVSMQIQRVLNSDIVMQFDECTPYEIDGRPATTEEAAKSMRMSLRWAKRSMDEFNREENPNALFGIVQGGMFENLRDESLAGLEELNFHGVAIGGLSVGEPKEDMMRVLEHVGPRLPANKPHYLMGVGTPEDLVAGVASGIDMFDCVMPTRNARNGWLFTRFGDIKIKNARYKDDKKPLDESCSCYACRNFSRAYLHHLHRTGEILGARLNTIHNLHYYLDLMREMREAISEGRFQLFVSQFHADRARGS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Klebsiella pneumoniae (strain 342)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.568 kDa
Sequence
MKFELDTTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTAPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGRTVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.98 kDa
Sequence
MAAIKYRLIKKDSRTNARLGILETPHGIIETPVFMPVGTQATVKSMTPEELKEIGATIILSNTYHLYLRPGHKIIEKAGGLHKFMNWDRAILTDSGGFQVFSLNSLRKITEDGVEFRSHIDGSRHFFTPEKVIEIQNALGSDIMMSFDECAPYPADYDYVKKSMELTIKWAERGKRAHKNTEKQALFGIVQGGTYEDLRKECAQRLVDMDFPGYSIGGLSVGEPKNVMYDIVDLTTEYLPEDKPRYLMGVGSPDDLIEGVIRGVDMFDCVLPTRIARNGTVFTSKGKLIVRDAPYAEDFSPLDEECDCYTCRNYSRAYIRHLFKANEILAARLATIHNLYFLIKLMERIREAIRQDRLLEFKKQFFKKYGYKEEY

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thermoanaerobacter sp. (strain X514)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.93 kDa
Sequence
MAAIKYRLIKKDSRTNARLGILETPHGVIETPVFMPVGTQATVKAMTPEELKEIGATIILSNTYHLYLRPGHKIIEKAGGLHRFMNWDRAILTDSGGFQIFSLSSLRKIKEEGVEFRSHIDGSKHFFTPEKVIEIQNALGSDIIMSFDECAPYPADYEYVKNSMELTIKWAERGKKAHKNTEKQALFGIVQGGIYEDLRKECAQRLVEMDFPGYSIGGLSVGEPKNVMYDIVDLTTEYLPENKPRYLMGVGSPDDLIEGVIRGVDMFDCVLPTRIARNGTVFTSKGKLIVRDAPYAEDFSPLDEECDCYTCKNYSRAYIRHLFKANEILAARLATIHNLYFLIKLMERIREAIRQDRLLEFKKQFFKKYGYKEEY

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.191 kDa
Sequence
MTTPGTFEIHATDGAARTGCLHTAHGIVRTPIFMPVGTVGSVKAIAPDDLEAIGAEIILGNTYHLYLRPGDELVARRGGLHEFNAWRKPILTDSGGFQVFSLSGLRRIAEEGVEFRSHLDGSKHLFTPEKVVSIQRNLNSDIMMVLDECVPYGADRTYTEKSVGLTTRWAKRCRDAYPKGAAGNLLFGITQGGFFKDLRTRSIGALTDIDFDGFALGGLSVGEPKAEMMDLLYHSAPLLPADKPRYLMGVGTPLDIINGIAAGVDMFDCVLPTRNARNGTLYTSLGKLNIKRREFAEDDGPLDPACSCYTCRTFSRAYLRHLYTAKELLAFRLNSIHNLTYFLDLVRGARAAIAAGRFAEYKRSFEAIYPEEVVA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Desulfovibrio vulgaris subsp. vulgaris (strain DP4)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.249 kDa
Sequence
MTTPGTFEIHATDGAARTGCLHTAHGIVRTPIFMPVGTVGSVKAIAPDDLEAIGAEIILGNTYHLYLRPGDELVARRGGLHEFNAWRKPILTDSGGFQVFSLSGLRRIAEEGVEFRSHLDGSKHLFTPEKVVSIQRNLNSDIMMVLDECVPYGADRTYTEKSVGLTTRWAKRCRDAYPKGAAGNLLFGITQGGFFKDLRTRSIGELTDIDFDGFALGGLSVGEPKAEMMDLLYHSAPLLPADKPRYLMGVGTPLDIINGIAAGVDMFDCVLPTRNARNGTLYTSLGKLNIKRREFAEDDGPLDPACSCYTCRTFSRAYLRHLYTAKELLAFRLNSIHNLTYFLDLVRGARAAIAAGRFAEYKRSFEAIYPEEVVA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli (strain 55989 / EAEC)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O157:H7
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O157:H7 (strain EC4115 / EHEC)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O81 (strain ED1a)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O8 (strain IAI1)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli (strain K12 / DH10B)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O9:H4 (strain HS)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O1:K1 / APEC
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli (strain K12)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli (strain SE11)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia coli (strain UTI89 / UPEC)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Enterobacter sp. (strain 638)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.753 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEVMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEKGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAQRSRDRFDSLENKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSTLDAECDCYTCRHYSRAYLYHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGRDVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.594 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPCFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRERFDSLGNKNALFGIIQGSVYEDLRDISVKGLVDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKYKSDTGPLDPECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGREVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella agona (strain SL483)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.522 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.453 kDa
Sequence
MKFELDTTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKCSMEMSLRWAKRSRDRFDGLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella choleraesuis (strain SC-B67)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.521 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTKFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella dublin (strain CT_02021853)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.536 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGIVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella enteritidis PT4 (strain P125109)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.536 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGIVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella gallinarum (strain 287/91 / NCTC 13346)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.536 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGIVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella heidelberg (strain SL476)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.522 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella newport (strain SL254)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.522 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.522 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQLPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.522 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella paratyphi C (strain RKS4594)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.521 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTKFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella paratyphi A (strain AKU_12601)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.522 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQLPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella schwarzengrund (strain CVM19633)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.522 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella typhi
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.534 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDISPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.522 kDa
Sequence
MKFELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTEFYQRQGRPVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.931 kDa
Sequence
MAAIKYQVIKKDARTKARLGILETPHGVIETPVFMPVGTQATVKAMTPDELKEMGATIILGNTYHLYLRPGHKIIEKAGGLHKFMNWDRAILTDSGGFQVFSLSSLRKITEDGVEFRSHIDGSKHFFTPEKVIEIQNSLGSDIIMSFDECAPYPADYDYVKRSMELTIKWAKRGKKAHKNTDRQALFGIVQGGTYKDLRRECAERLVDMDFPGYAIGGLSVGEPKDLMYEIIDFTTDYLPHDKPRYLMGVGTPEDLIEGVIRGVDMFDCVLPTRIARNGTVFTSRGKLIVRDAPYAEDFSPLDEECDCYTCKNYSRAYLRHLFKAKEILAARLATYHNLYFLIKLMEKIREAIRQDRLLEFKEEFLKKYYGNREE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Pseudoalteromonas haloplanktis (strain TAC 125)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.722 kDa
Sequence
MKFELDTTDGKARRGRLIFDRGVIETPAFMPVGTYGTVKGMTPDEVKATGAQVCLGNTFHLMLRPGTEIIKQHGGLHKFMNWDFPILTDSGGFQVFSLGAMRKITEEGVLFSSPVNGEKIMMTPESSMQVQRDLGSDIVMIFDECTPYPATEKEAKDSMELSLRWAKRSKEGHGDNPSALFGIIQGGMYPELRAQSQAGLEEIGFDGYALGGLSVGEPKNEMINILDHCAYKMPADKPRYLMGVGKPEDLVESVRRGIDMFDCVMPTRNARNGHLFITTGVVKIRNAVHKTDTGPLDPECDCHTCGNYSRAYLHHLDKCNEILGARLNTIHNLRYYQRVMEGLRNAISAGKLDEFVQDFYARRGQDVPELADITN

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.101 kDa
Sequence
MLRFDLLHTEGHARRGRLTLNHGVVETPIFMPVGTYGTVKGVMPASLEAMGAQIILGNTFHLWLRPGLDVLRQFGGLHRFENWQRPILTDSGGFQVWSLGAMRKISEEGVKFASPVNGDKLFLTPETSMQIQTVLNSDIVMQFDECTPYETSGHLTTEQEARASMELSLRWAARCKTEFARLENPNALFGIVQGGMFEPLRQASLDALVAMDFPGYAIGGVSVGEPKDEMLRIMAHTPHRLPAHKPRYLMGVGTPEDLVEGVTQGVDLFDCVMPTRNARNGHLFTRHGDLRLRNARYKTDERPIDESCTCTACNGFSRAYLHHLDRCGEMLGPMLTSIHNLHYFLNLMREVREALDAGRFEAFRAQFRADRARGV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Borreliella bavariensis (strain ATCC BAA-2496 / DSM 23469 / PBi)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.064 kDa
Sequence
MFSVIKNDKHSNARVGFLNLPHGRVDTPCFMPVGTLGAMKGLKHSVLEKLKCNLMLANTYHLYLRPGIKTIEKYGGLHNFTTWNKNFLTDSGGFQVFSLSSLRKIDLKGVRFKSHLDGSYHYFTPEGVFAMQEIFGSDIIMPLDICSSYGIDYNEANLYTNITTNWARSTFKAYKNRKEGYNGLLFLITQGNFFKDLRKRSINDILELDSPGIAIGGISVGEPREKYLEILEYSSLLMPKEKPRYVMGIGTPHYILDAIYHGIDIFDCVNPARIARHGSLLTDNGIMRISRKEYKDDTSQVEKNCGCTLCTRYSRGYLRHLIKSKELFGIILASEHNIYYMFRLISKIRTAILNDNFLNFRTSYLKKYEEENFDE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.199 kDa
Sequence
MFSVIKNDKHFNARVGFLNLPHGRVDIPCFMPVGTLGAMKGLKHAVLEKLECNLMLANTYHLYLRLGIKTVEKYVGLHNFTIWNKNFLTDSGGFRVFSFSDLRKIDLKGVHFKSHIDGSYHYFTSEGIFAMQEIFGSDIIMPLDICSSYGIDYNEANLYTNITTNWASSTFKSSKNRKEGYNGLLFLITQGNFFKDLRKRSINDILELDSPGIAIGGISVGEPREKYLEILEYSFLLIPKEKPRYVMGIGTPHYILNAIYYGIDIFDCFNPARITRHGSLLTDNGIMCIGRKEYKDDTSKVEKNCICTLCKRYSRGYLRHLIKSKELFGIVLASEHNIHYMFRLISKIRAAILNDDFLNFRTSYLKKYEEENFDE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Borrelia burgdorferi (strain ZS7)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
43.247 kDa
Sequence
MFSVIKNDKHFNARVGFLNLPHGRVDIPCFMPVGTLGAMKGLKHAVLEKLECNLMLANTYHLYLRLGIKTVEKYVGLHNFTTWNKNFLTDSGGFRVFSFSDLRKIDLKGVHFKFHIDGSYHYFTSEGIFAMQEIFGSDIIMPLDICSSYGIDYNEANLYTNITTNWASSTFKSSKNRKEGYNGLLFLITQGNFFKDLRKRSINDILELDSPGIAIGGISVGEPREKYLEILEYSFLLIPKEKPRYVMGIGTPHYILNAIYYGIDIFDCFNPARITRHGSLLTDNGIMCIGRKEYKDDTSKVEKNCICTLCKRYSRGYLRHLIKSKELFGIVLASEHNIHYMFRLISKIRAAILNDDFLNFRTSYLKKYEEENFDE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Borrelia duttonii (strain Ly)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.947 kDa
Sequence
MFNIIKNDKNSNARLGILELPHGNVATPCFMPVGTLGVMKALKHDVLEKLGCDLMLANTYHLYLRPGIDVIKKYGNLHNFTTWNKNFLTDSGGFQVFSLSNFRKIEDEGVDFKSHIDGSRHYFTPESVFSMQETFESDIIMALDICSPYGIDYDEASLYTNITTSWARRTLCAYKNRKEGYEGLLFLITQGNFFKDLRKRSTESILELNSPGIAIGGISVGEPRDRYLEILEYNSSLIPKDKPKYVMGIGTPHYILDAIYNGIDIFDCVNPTRIARHGSLLTDNGILRINRAEFRFDTCSVERECSCTLCTRYSRGYLRHLFKSEEALGVMLASEHNIHYMFRLINKAKNAIMNDNFVKFRKLYLDKYDEGNLNE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Borrelia hermsii (strain HS1 / DAH)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.793 kDa
Sequence
MFNIIKNDKNSNARIGVLELPHGKVTTPCFMPVGTLGVMKALKHDVLEKLGCNLMLANTYHLYLRPGIDVIKEYGSLHNFTTWNKNFLTDSGGFQVFSLSNFRKIETEGVDFKSHIDGSRHYFTPESVFKMQEIFESDIIMALDICSSYGIDYSEASLYANITTSWARRTLRAYENRKEGYDGFLFLITQGNFFKDLRKRSTEAILELNSPGIAIGGISVGEPRDKYLEILEYNSSLIPKDKPKYVMGIGTPHYILDAIYYGIDIFDCVNPTRIARHGSLLTDNGILRIKRAGFNVDTSPIEQDCSCTLCTRYSRGYLRHLIKSGETLGVMLASEHNIHYMFRLIQKARNAIMNDDFTQFRKLYLSKYDEGNFNE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Borrelia recurrentis (strain A1)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.95 kDa
Sequence
MFNIIKNDKNSNARLGILELPHGNVATPCFMPVGTLGVMKALKHDVLEKLGCDLMLANTYHLYLRPGIDVIKKYGNLHNFTTWNKNFLTDSGGFQVFSLSNFRKIEDEGVDFKSHIDGSRHYFTPESVFSMQETFESDIIMALDICSPYGIDYDEASLYTNITTSWARRTLCAYKNRKEGYEGLLFLITQGNFFKDLRKRSTELILELNSPGIAIGGISVGEPRDRYLEILEYNSSLIPKDKPKYVMGIGTPHYILDAIYNGIDIFDCVNPTRIARHGSLLTDNGILRINRAEFCFDTCSVERECSCTLCTRYSRGYLRHLFKSEEALGVMLASEHNIHYMFRLINKTKNAIMNDNFVKFRKLYLDKYDEGNLNE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Borrelia turicatae (strain 91E135)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.867 kDa
Sequence
MFSIIKNDKNSNARLGVLELPHGKVETPCFMPVGTLGAMKALKHDVLEKLGCDLMLANTYHLYLRPGIDVIKKYGSLHNFTAWDKNFLTDSGGFQVFSLANFRKIETEGVDFKSHIDGSRHYFTPESVFKMQEIFESDIIMALDICSSYGIDYSEASLYTNITTSWARRTLRAYENRKEGYDGLLFLITQGNFFKDLRKRSTEAILELDSPGIAIGGISVGEPRDKYLEILEYNSSLIPKVKPKYVMGIGTPHYILDAIYYGIDIFDCVNPTRIARHGSLLTDNGILRIKRAEFNFDTCPVERDCSCTLCTRYSRGYLRHLIKSEETLGVMLASEHNIHYMFRLIKKARNAIMNGDFTKFRKLYLSKYDEGNFDE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Length
375 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.568 kDa
Sequence
MKFELDTTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILTDSGGFQVFSLGDIRKITEQGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLGNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTAPLDAECDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGRTVPPLNVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.678 kDa
Sequence
MSAIFSFQSLARCSQTKARSGIFLTPHGIVETPRFMPVGTLANVKTVTPAQLKETGAQMVLSNTYHLHLQPGEAIVAGGGGLHKFMGWNGPMLTDSGGFQVFSLSEMRKITEEGVTFRSPRDGQIIKLTPERSIEIQNILGADVIMAFDECPPYPANRQEVEAATERTYRWLERCITAHQRQDQALFGIVQGGVYLDLRAKAANTLTELDLPGYAIGGVSVGEPPEMMAQIVQATAPLLPAHKPRYLMGVGTYREMVIAIASGIDLFDCVIPTRWARHGTAMVKGERWNLKNAKFREDFAPIDETCPCYACQNFSRAYISHLVRSQEILAYTLLSIHNITELIRFTQKIREAILSDRFLEEFGHWLNSAETDNR

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.389 kDa
Sequence
MTRFSFKIHATDGKARTGAIQMMRGEIRTPAFMPVGTAATVKAMKVEDVRASGADIILGNTYHLMLRPGAERVARLGGLHKFMGWDRPILTDSGGYQVMSLSDLRKITEEGVTFASHLDGSRHLLSPERSMEIQRLLGSDIVMCFDECPRADQPREVIARSMEMSMRWARRSRDAFDAGGEHAERSALFGIQQGALDEGLRKTSADALTDIGFDGYAIGGLAVGEGQEAMFATLDFAPQQLPADRPRYLMGVGKPDDLVGAVERGVDMFDCVLPTRSGRNGQAFTWNGPLNMRNARHAEDTGPLDERCPCPTCTKYSRAYLHHLHKSGEMLGAMLLTEHNLWFYQQLMAGMRAAIAEGRFAAFAADFRRDYFAR

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.737 kDa
Sequence
MKFELQTTDGQARRGRLIFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHGFMQWHGPILTDSGGFQVFSLGAMRKIKEEGVHFRNPINGTPVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAARSRKRFDELQNKNALFGIIQGSIYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPQDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTHGVIKIRNAKHKEDTSPLDEQCDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAKIRQAIEEGNLEQFVEDFYQRIGKPVPALSI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.633 kDa
Sequence
MKYELQKTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWHGPILTDSGGFQVFSLGAMRKIKEEGVHFKNPINGDSVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAARSRQRFDELNNKNALFGIIQGGVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDTATLDEHCDCYTCRHYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLEHFVEDFYGRIGKPVPPLNV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Yersinia pestis bv. Antiqua (strain Antiqua)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.633 kDa
Sequence
MKYELQKTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWHGPILTDSGGFQVFSLGAMRKIKEEGVHFKNPINGDSVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAARSRQRFDELNNKNALFGIIQGGVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDTATLDEHCDCYTCRHYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLEHFVEDFYGRIGKPVPPLNV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Yersinia pseudotuberculosis serotype IB (strain PB1/+)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.633 kDa
Sequence
MKYELQKTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWHGPILTDSGGFQVFSLGAMRKIKEEGVHFKNPINGDSVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAARSRQRFDELNNKNALFGIIQGGVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDTATLDEHCDCYTCRHYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLEHFVEDFYGRIGKPVPPLNV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Yersinia pestis
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.633 kDa
Sequence
MKYELQKTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWHGPILTDSGGFQVFSLGAMRKIKEEGVHFKNPINGDSVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAARSRQRFDELNNKNALFGIIQGGVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDTATLDEHCDCYTCRHYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLEHFVEDFYGRIGKPVPPLNV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Yersinia pestis bv. Antiqua (strain Angola)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.633 kDa
Sequence
MKYELQKTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWHGPILTDSGGFQVFSLGAMRKIKEEGVHFKNPINGDSVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAARSRQRFDELNNKNALFGIIQGGVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDTATLDEHCDCYTCRHYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLEHFVEDFYGRIGKPVPPLNV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Yersinia pestis bv. Antiqua (strain Nepal516)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.633 kDa
Sequence
MKYELQKTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWHGPILTDSGGFQVFSLGAMRKIKEEGVHFKNPINGDSVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAARSRQRFDELNNKNALFGIIQGGVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDTATLDEHCDCYTCRHYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLEHFVEDFYGRIGKPVPPLNV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Yersinia pestis (strain Pestoides F)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.633 kDa
Sequence
MKYELQKTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWHGPILTDSGGFQVFSLGAMRKIKEEGVHFKNPINGDSVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAARSRQRFDELNNKNALFGIIQGGVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDTATLDEHCDCYTCRHYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLEHFVEDFYGRIGKPVPPLNV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.633 kDa
Sequence
MKYELQKTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWHGPILTDSGGFQVFSLGAMRKIKEEGVHFKNPINGDSVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAARSRQRFDELNNKNALFGIIQGGVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDTATLDEHCDCYTCRHYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLEHFVEDFYGRIGKPVPPLNV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Yersinia pseudotuberculosis serotype O:3 (strain YPIII)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.633 kDa
Sequence
MKYELQKTDGRARRGRLVFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWHGPILTDSGGFQVFSLGAMRKIKEEGVHFKNPINGDSVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAARSRQRFDELNNKNALFGIIQGGVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDTATLDEHCDCYTCRHYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRQAIEEGKLEHFVEDFYGRIGKPVPPLNV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Serratia proteamaculans (strain 568)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.494 kDa
Sequence
MKYELDTTDGRARRGRLIFERGVVETPAFMPVGTYGTVKGMTPEEVKETGAQILLGNTFHLWLRPGQEIMKLHGDLHDFMQWHGPILTDSGGFQVFSLGAMRKIKEEGVHFRNPINGDKVFLSPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKSSMEMSLRWAQRSRQRFDELNNKNALFGIIQGGVYEDLRDVSVKGLVDIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKDDTSPLDKDCDCYTCRNYSRAYLHHLDRCNEILGARLNTIHNLRHYQRLMAGLREAIEQGKLELFVADFYGRIGKPVPPLNA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.519 kDa
Sequence
MKFELITTQGRARRGRLVFERGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFMDAEKSMQIQHSLGSDVVMIFDECTPYPATHDEARKSMQMSLRWAKRSRDEFDRLENPNSLFGIIQGSVYEDLRDESLKGLLEIGFDGYAVGGLAVGEPKEDMHRVLEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDPKCDCYTCTNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMEGLRGAIETGTLDAFVADFYTSQGREVPELKD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella baltica (strain OS223)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.413 kDa
Sequence
MKFELDTTDGRARRGRLIFDRGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQDALGSDVVMIFDECTPYPATEDEARKSMQMSLRWARRSRDEFDRLENPNSLFGIIQGGVYEDLRDESLKGLVDIGFDGYAVGGLAVGEPKADMHRILEHICPQIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDTKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVADFYTSQGREVPELVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella baltica (strain OS155 / ATCC BAA-1091)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.413 kDa
Sequence
MKFELDTTDGRARRGRLIFDRGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQDALGSDVVMIFDECTPYPATEDEARKSMQMSLRWARRSRDEFDRLENPNSLFGIIQGGVYEDLRDESLKGLVDIGFDGYAVGGLAVGEPKADMHRILEHICPQIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDTKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVADFYTSQGREVPELVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella baltica (strain OS185)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.412 kDa
Sequence
MKFELDTTDGRARRGRLIFDRGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQDALGSDVVMIFDECTPYPATEDEARKSMQMSLRWARRSRDEFDRLENPNSLFGIIQGGVYEDLRDESLKGLVDIGFDGYAVGGLAVGEPKADMHRILEHICPQIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDTKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVADFYTSQGREVPELVN

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella baltica (strain OS195)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.413 kDa
Sequence
MKFELDTTDGRARRGRLIFDRGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQDALGSDVVMIFDECTPYPATEDEARKSMQMSLRWARRSRDEFDRLENPNSLFGIIQGGVYEDLRDESLKGLVDIGFDGYAVGGLAVGEPKADMHRILEHICPQIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDTKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVADFYTSQGREVPELVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella frigidimarina (strain NCIMB 400)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.451 kDa
Sequence
MKFELDTTDGRARRGRLIFDRGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQDSLGSDVVMIFDECTPYPATHDEARKSMQMSLRWAKRSRDEFDRLENPNSLFGIIQGGVFEDLRDESVKGLLDIGFDGYAVGGLAVGEPKADMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTATLDPKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVKEFYTSFGREVPELIV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.596 kDa
Sequence
MKFELDTTDGRARRGRLVFERGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFMDAEKSMQIQYSLGSDVVMIFDECTPYPATHDEARKSMQMSLRWAQRSRDEFDRLENPNSLFGIIQGSVYEDLRDESLKGLLEIGYDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDAKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVEEFYTSQGREVPKLSD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella oneidensis (strain MR-1)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.578 kDa
Sequence
MKFELDTTDGRARRGRLIFDRGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQHALGSDVVMIFDECTPYPATEDEARKSMQMSLRWAKRSRDEFDRLENPNSLFGIIQGSVYEDLRDESLKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQILADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDPKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVKDFYTSQGREVPELVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella putrefaciens (strain CN-32 / ATCC BAA-453)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.398 kDa
Sequence
MKFELDTTDGRARRGRLIFDRGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQDALGSDVVMIFDECTPYPATEDEARKSMQMSLRWAKRSRDEFDRLKNPNSLFGIIQGGVYEDLRDESLKGLVEIGFDGYAVGGLAVGEPKADMHRILEHICPQIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDTKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVADFYTSQGREVPELVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella sp. (strain ANA-3)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.576 kDa
Sequence
MKFELDTTDGRARRGRLIFERGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQHALGSDVVMIFDECTPYPATEDEARKSMQMSLRWAKRSRDEFDRLENPNSLFGIIQGSVYEDLRDESLKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDPKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVKDFYTSQGREVPELVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella sp. (strain MR-4)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.576 kDa
Sequence
MKFELDTTDGRARRGRLIFERGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQHALGSDVVMIFDECTPYPATEDEARKSMQMSLRWAKRSRDEFDRLENPNSLFGIIQGSVYEDLRDESLKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDPKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVKDFYTSQGREVPELVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella sp. (strain MR-7)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.576 kDa
Sequence
MKFELDTTDGRARRGRLIFERGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQHALGSDVVMIFDECTPYPATEDEARKSMQMSLRWAKRSRDEFDRLENPNSLFGIIQGSVYEDLRDESLKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDPKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVKDFYTSQGREVPELVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Shewanella sp. (strain W3-18-1)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.398 kDa
Sequence
MKFELDTTDGRARRGRLIFDRGTVETPAFMPVGTYGTVKGMTPEEVRATGADILLGNTFHLWLRPGEEIMRKHGDLHDFMNWQRPILTDSGGFQVFSLGDIRKITEEGVHFRSPINGEKIFLDPEKSMQIQDALGSDVVMIFDECTPYPATEDEARKSMQMSLRWAKRSRDEFDRLKNPNSLFGIIQGGVYEDLRDESLKGLVEIGFDGYAVGGLAVGEPKADMHRILEHICPQIPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFTSEGVIKIRNARHRDDTSPLDTKCDCYTCKNYSRAYLYHLDRCNEILGARLNTIHNLRYYQMLMEGLRGAIETGTLDAFVADFYTSQGREVPELVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.568 kDa
Sequence
MSAIRYELIKKCKQSGARLGRVYTPHGCFDTPAFMPVGTQATVKGMSPDEMKEIEAQIILSNTYHLHMRPGEDIVKEAGGLHGFMNWDRPILTDSGGFQVFSLSDLRDIKEEGVTFKSHIDGSKHFISPEMAIKIQNDLGADIIMAFDECIPYPADYDYAKKSLERTTRWAKRCKDAHRNPEKQALFGIVQGGMYKDLRQQSAYELLELDFPGYAIGGLSVGEPAEIMYEMLEVTVPLLPEDKPRYLMGVGSPDYLIEGATRGIDMFDCVLPTRIGRNGTVLTSKGRIIVRDAIYARDYTPIDPECDCYACRNFTRAYIRHLLKSGEVLGIRLTTWHNLRFLINLMKKVRQAIMEDRLLDFRDEFFSKFGYKKI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.409 kDa
Sequence
MKFELTTTDGDARRGQLTFSRGTVQTPAFMPVGTYGTVKGMLPRDIVDSGAEIILGNTFHLMLRPGTEVVKAHGDLHDFIQWQGPILTDSGGFQVFSLGDMRKISEEGVKFRSPIDGSEVFLDPEKAMQVQRDLGSDIVMIFDECTPYPATVHEARVSMELSLRWAKRSKDAHGDNPSALFGIVQGGMHESLRSESLKGLTEIGFDGYAIGGLSVGEPKEDMLRILNHLKTEMPADKPRYLMGVGKPEDLVEGVCRGIDMFDCVMPTRNARNGHLFTQAGVVKIRNAKHRHDTGPLDPTCDCYTCQNFSRAYLHHLDKCGEILGAQLNTIHNLRHYQTVMSELRAAIGKGELAQYVSHFYARQGKERPAIATQS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Campylobacter fetus subsp. fetus (strain 82-40)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.297 kDa
Sequence
MNFKIDKTDGNARACTLQTAHSTIQTPIFMPVGTLGAVKSLDAIDLKEILDAKIILANTYHLYLRPTSKVVREFGGLHGFSKFDRSFLTDSGGFQAFSLSKISKPDENGIKFKSHIDGSMHYFTPKSVLDTQYDLSSDIMMILDDLVALPATKERIDLSIKRTINWAKIACEYHKSNKQKSVGIDQNIFGIIQGGTDYNARKLCAEALCEMEFDGLAIGGLSVGESNEEMYDTVEALMPFIDKNRPRYLMGVGTPEDLVQNVERGVDMFDCVMPTRNARNGTLFTSFGKINIKSAAFIKDDNKIDPECDCYTCSNFSRGYLNHLYKARELTFFRLASLHNLHYYLNLVKQMREAIMQGKFKEFKREFYAKRGMI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Psychromonas ingrahamii (strain 37)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.488 kDa
Sequence
MEYKLINTDGRARRGRLTFDRGSVETPAFMPVGTYGTVKGMTPEEVDATGAEILLGNTFHLWLRPGQKVIKAHGDLHDFMNWKGPILTDSGGFQVFSLGKMRKIKEEGVYFRSPINGSEVFLSPEISMDIQYDLGSDIVMIFDECTPYPATEEETDVSMQLSLRWAQRSRDRFDEQQNPNALFGIIQGGCFEQFRDISLDGLTNIGFDGYAIGGLAVGEPKEDMYRILEYIAPKIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFTTDGVIKIRNAKHREDATTLDSECDCYTCKNYTRAYLYHLDKCGEILGARLNTIHNLSYYQRLMKGLREAIEQGKLEDFVDTFYQRIGKEKPMLDV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.499 kDa
Sequence
MPLPSVNFTYQCQARCSHSQARAGIFQTPHGPVETPRFMPVGTLATVKGITPAQLADTQAQMVLANTYHLHLQPGEKIIAAAGGVHKFMGWSGPMLTDSGGFQVFSLSQLRTIGEQGVLFRSPRDGRLIDMTPENSIRIQNALGADVIMAFDECPPGQGDRLMVEQATARTYRWLERCIEAHQRPGDQALFGIVQGGTYLDLRSQAAEQLIALDLPGYAIGGVSVGEAPALIDKVVQHTAPLLPAHKPRYLMGVGTYREMARAIFAGIDLFDCVIPTRFGRHGTALVQGERWNLKNATFREDHRPLDETCPCYTCQTFSRAYLNHLIRSREMLGYILLSLHNITELIRFTQSIRQAILNDTFTQDFAHWLTPPE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.479 kDa
Sequence
MIFQTTSEDLRTRARTGILNLNGVKLETPVFMPVGTRGVVKTISADDLEELEYSLILGNTYHLYLRPGTAVLERFGGLKKFSTWKRALLTDSGGYQVFSLNSLFKYEQDGVRFQSHIDGSRHYFTPNSVIDIQRTIGSDIMMVLDDCAPFDSSQERLRQSLDRTHRWAEMSVEYWEKNKNSSHLFGIFQGGIDLGLRLESLQKIVSLPFDGIAIGGLSVGEPRKDFIRILEGVSAYTDRSRPLYLMGVGTVPDILDGVKNGVDMFDCVLPTRNARNGQVFTSLGKINLRNEKWKSSDVPIDPHCGCKVCKRYSIGYIRHLHHVGELTAFSLSTYHNLYFMKNFLSEIRKSIQAGEFLKIYAKWKNLYEKPEFSG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain L550)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.479 kDa
Sequence
MIFQTTSEDLRTRARTGILNLNGVKLETPVFMPVGTRGVVKTISADDLEELEYSLILGNTYHLYLRPGTAVLERFGGLKKFSTWKRALLTDSGGYQVFSLNSLFKYEQDGVRFQSHIDGSRHYFTPNSVIDIQRTIGSDIMMVLDDCAPFDSSQERLRQSLDRTHRWAEMSVEYWEKNKNSSHLFGIFQGGIDLGLRLESLQKIVSLPFDGIAIGGLSVGEPRKDFIRILEGVSAYTDRSRPLYLMGVGTVPDILDGVKNGVDMFDCVLPTRNARNGQVFTSLGKINLRNEKWKSSDVPIDPHCGCKVCKRYSIGYIRHLHHVGELTAFSLSTYHNLYFMKNFLSEIRKSIQAGEFLKIYAKWKNLYEKPEFSG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.433 kDa
Sequence
MIFQTTSEDTLTKARTGILNLNGIELKTPVFMPVGTRGVVKTLSADDLEELEYSLILGNTYHLYLRPGTSVLDRFGGLKKFSTWKKALLTDSGGYQVFSLNSLFKYEQDGVRFQSHIDGSRHYFTPNSVIDIQRSIGSDIMMVLDDCAPFDSGPERLKQSLDRTHRWAEMSVQYWEKNKNSQHLFGIFQGGIDLDFRLESLNTITSLPFDGIAIGGLSVGEPRKDFIRILDGISAHTDRNRPLYLMGVGTVPDILDGVKNGVDMFDCVLPTRNARNGQVFTTLGKINLRNEKWKSSDTPMDPNCTCKVCKRYSIGYIRHLHHVGEITAFSLSTYHNLHFMKNFLTEIQNSIQKGEFLEIYAKWKNLYEKPEFSG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Length
374 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.433 kDa
Sequence
MIFQTTSEDTLTKARTGILNLNGIELKTPVFMPVGTRGVVKTLSADDLEELEYSLILGNTYHLYLRPGTSVLDRFGGLKKFSTWKKALLTDSGGYQVFSLNSLFKYEQDGVRFQSHIDGSRHYFTPNSVIDIQRSIGSDIMMVLDDCAPFDSGPERLKQSLDRTHRWAEMSVQYWEKNKNSQHLFGIFQGGIDLDFRLESLNTITSLPFDGIAIGGLSVGEPRKDFIRILDGISAHTDRNRPLYLMGVGTVPDILDGVKNGVDMFDCVLPTRNARNGQVFTTLGKINLRNEKWKSSDTPMDPNCTCKVCKRYSIGYIRHLHHVGEITAFSLSTYHNLHFMKNFLTEIQNSIQKGEFLEIYAKWKNLYEKPEFSG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Nitratiruptor sp. (strain SB155-2)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.196 kDa
Sequence
MDFFIDATDNNARACTIKTSHSTIKTPVFMPVGTAASVKSLDTVDLRDILQTQIILANTYHLYLRPGDNVVKKLGGLHGFTGYNRSFLTDSGGFQAFSLSDISKANERGIEFQSHIDGSKHFFTPQKVLDIQYNLGSDIMMILDDLVALPATKERLALSVDRTTRWAQESIKYHKKMQAQGIGTNQNIFAIIQGGTDYEFRKKSAMELTALDFDGFAIGGLSVGEENSVMYNTVEFTTPFMPKNKPRYLMGVGTPEDLVECIDRGVDMFDCVMPTRNARNGTIFTSFGRLNIKAAKYKLDQNPIDEACSCYTCQNYTRAYLNHLYRAKELTYYRLASIHNLHYYLTLMKEAREAIEKGEYKAFKKAFYARRQS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.208 kDa
Sequence
MAAVTYELIKTCKQTGARLGKVHTPHGSFDTPVFMPVGTLATVKGMSPEELKEIDARIILSNTYHCYLRPGQDIVKQAGGLHGFMNWDRPILTDSGGFQVFSLSGLRKITEEGVTFRSHLDGSKHVFTPESVMDIENDLGADIIMAFDECAPYPAEYDYVKKSMERTTRWAKRCKEAHTNTEKQSLFGIIQGGMYKELRIESANQLKELDFPGYAIGGLSVGEPAEIMYEVLDYTAPLMPADKPRYLMGVGTPDYLIEGAIRGIDMFDCVLPTRIGRNGTVLTSNGRVIIRDAKYSRDFSKLDPECDCYVCRNYSRAYIRHLIKCGELLGLRLTTWHNLYFLINLMKQVRQAIMDDKLASFRDEFYLKYGYTK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.8 kDa
Sequence
MKLPVTYKVEDKDGKARAGVITTLHGEIETPVFMPVGTQATVKTMSKEELLDIGSEIILGNTYHLYLRPNDELIARLGGLHKFMNWDRPILTDSGGFQVFSLGSLRKIKEEGVYFSSHIDGSKHFISPEKSIQIQNNLGSDIVMLFDECPPGLSTREYIIPSIERTTRWAKRCVEAHQKKDIQGLFAIVQGGIYEDLRQKSLDELSEMDENFSGYAIGGLAVGEPREDMYRILDYIVEKCPEEKPRYLMGVGEPVDMLNAVESGIDMMDCVQPTRLARHGTVFTKDGRLVIKSERYKEDTKPLDEECDCYVCKNYSRAYIRHLIKVQEVLGLRLTSYHNLYFLIKLMKDAREAIKEKRFKEFKEKFIQRYEGK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.634 kDa
Sequence
MSISFNLLHREINTRARLGKLKTPHGDIDTPIFMPVGTQATVKSMTPDELENIKAQIILSNTYHLYLRPGSSLIDEAGGLHNFMNWQKPILTDSGGFQVFSLSDLREIKEEGVYFRSHLDGSRHFISPEKAIQIQMELGADIIMAFDECPPYPSDYDYVARSLERTVRWARRCKKAHEREDQALFGIIQGGVYRDLRKQSVEALIDIGFPGYAIGGLSVGEEKEKMLEVLDFTVPLMPENKPRYLMGVGAPEDLVEGVIRGVDMFDCVLPTRIARHGTVFTSQGRLTVRNAGYERDFTPLDPECDCYVCKNYTRAYIRHLIKRKEILGVRLTTYHNLYFLLSLMEKIRGAIKEDALLEFRDEFLRKYLNKASI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.162 kDa
Sequence
MTMKFELDKTSGRARRGRMVFERGTVETPAFMPVGTLGTVKGMTPEEVKDTGAQICLGNTFHLMLRPGTQIIQQHGDLHDFMNWDKPILTDSGGFQVFSLGELRKITEEGVTFRSPINGEKILLTPEKSMQVQRELGSDIVMIFDECTPFPATQAEARSSMELSLRWAERSKQEHGESKAALFGIIQGGMYEELRDISLKGLTDIGFDGYAIGGLSVGEPKEDMMRILEHTAPQMPEQKPRYLMGVGKPEDLVEAVRRGIDMFDCVMPTRNARNGHLFISTGVVKIRNAVHRTDTSPLDENCDCYTCKNYSRAYLHHLDRTNEMLGSRLNTIHNLRFYQKVMSDMRDALDAGTFDDYVKEFYRLRDQSVPALD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Tolumonas auensis (strain DSM 9187 / TA4)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.449 kDa
Sequence
MKFELKKTEGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVKDTGAQILLGNTFHLWLRPGQDIMRKHGDLHDFMNWHGPILTDSGGFQVFSLGHIRKIKEEGVHFRNPINGEKIFLSPEKSMEIQNDLGSDVVMIFDECTPYPATHDVAKKSMEMSLRWATRSRQRFDELENKNALFGIIQGGVYEDLRDVSLKGLLDIGFDGYAVGGLAVGEPKEDMHRILKHVCPQIPEDKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFTTDGVVKIRNAKYKDDVTSLDAECDCYTCKNYTKSYLHHLDRCNEMLGARLNTIHNLRYYQRLMQGLRDAIDAGTLDDFVADFYQRQDKPVPSLD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Desulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.167 kDa
Sequence
MNAPGTFTLGPGDGSARTARLTTAHGEIETPVFMPVGTQGTVKSLCPTDLQDIKARIILGNTYHLYLRPGDELVAKLGGLHRFMGWDGPILTDSGGFQVFSLSGLRRITEEGVTFASHIDGSKHLFSPEKVVSIQRNLGSDIMMVLDECVPYGADRAYTEKSLGLTTRWARRCRKAHPAGDRGQLMFGIVQGGFFKDLRAQSAEQIIEVGFDGYALGGLSVGESRAEMYDILGDAAPLLPADRPRYLMGVGAPRDLLAGMAAGIDMFDCVLPTRNARNGTLFTFQGKVNIKRAEYREDDSPLDPTCPCYACRTFSRAYLRHLYIAKELLSYRLNTLHNLTFFSIMMERARQAIREGRFAAYRAEMEALYPEGE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Arcobacter butzleri (strain RM4018)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.219 kDa
Sequence
MEFKIDGTSQGARACTIKTAHSTILTPVFMPVGTQGTVKALDANDMLELGAKIILGNTYHLYLRPGSKLIKKFGGLHGFSKFPNSFLTDSGGFQAFSLSNNSKPDENGITFKSHIDGSRHYFTPKSVLDTQYDLNSDIMMILDDLVALPNTDERIKTSIQRTTKWAQEAINYHMEQKQKGIGTHQNIFAIIQGGTSKEFRKLSAQQLCDMSDFDGFAIGGLSVGEPNEQMYETVEWTTQFMPKDKPRYLMGVGTPEDLIENIERGVDMFDCVMPTRNARNGTLFTSFGKLNIKKAEFKDDANPIDNECSCYTCKNFSRAYLNHLFRAAEITYFRLASIHNIHYYLNLMKQAREAILADNWSEFKKEFYVKRSK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.445 kDa
Sequence
MEFKLKHKDGMARVCEITTAHSTFLTPVFMPVGTVGAVKSLDANDMKNELDAKIILANTYHMYLRPTSKVVKDFGGLHGFTKFDRSFLTDSGGFQAFSLSKNSKHFNEGIEFKSHIDGSRHLFTPKSVLDTQYDFNSDIMMILDDLVALPATKERVKISVDRTILWAKEAITYHKSMQNKGIGIGQNIFGIIQGGTDYKERKRCALSLNEMPFDGLAIGGLSVGEENALMYETVQNLNPYLDENRPRYLMGVGTPEDLVENVERGVDMFDCVMPTRNARNGTFFTSFGKFNIKKAEFINDHEAIDPACSCYTCCNFSRGYLNHLFKAKELTFFRLASLHNLHYYLELARKMREAILNNSFTQFKRNFYHLRGK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.437 kDa
Sequence
MEFKLKHKDGMARVCEITTAHSTFLTPVFMPVGTVGAVKSLDANDMKNELDAKIILANTYHMYLRPTSKVVKDFGGLHGFTKFDRSFLTDSGGFQAFSLSKNSKHFNEGIEFKSHIDGSRHLFTPKSVLDTQYDFHSDIMMILDDLVALPATKERVKISVDRTILWAKEAITYHKSMQNKGIGIGQNIFGIIQGGTDYEERKRCALSLNEMPFDGLAIGGLSVGEENALMYETVQNLNPYLDENRPRYLMGVGTPEDLVENVERGVDMFDCVMPTRNARNGTFFTSFGKFNIKKAEFINDHEAIGPACSCYTCRNFSRGYLNHLFKAKELTFFRLASLHNLHYYLELAREMREAILNNSFTQFKKNFYHLRGK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.574 kDa
Sequence
MEFKLKHKDGMARVCEITTAHSTFLTPVFMPVGTVGAVKSLDANDMKNELDAKIILANTYHMYLRPTSKVVKDFGGLHGFTKFDRSFLTDSGGFQAFSLSKNSKHFNEGIEFKSHIDGSRHLFTPKSVLDTQYDFNSDIMMILDDLVALPATKERVKISVDRTILWAKEAITYHKNMQNKGIGIGQNIFGIIQGGTDYEERKRCALSLNEMPFDGLAIGGLSVGEENALMYETVQNLNPYLDENRPRYLMGVGTPEDLVENVERGVDMFDCVMPTRNARNGTFFTSFGKFNIKKAEFINDHEVIDSTCSCYTCRNFSRGYLNHLFKAKELTFFRLASLHNLHYYLELARKMREAILNNSFTQFKRNFYHLRGK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.48 kDa
Sequence
MEFKLKHKDGMARVCEITTAHSTFLTPVFMPVGTVGAVKSLDANDMKNELDAKIILANTYHMYLRPTSKVVKDFGGLHGFTKFDRSFLTDSGGFQAFSLSKNSKHFNEGIEFKSHIDGSHHLFTPKSVLDTQYDFNSDIMMILDDLVALPATKERVKISVDRTILWAKEAITYHKSMQNKGIGIGQNIFGIIQGGTDYEERKRCALSLNEMPFDGLAIGGLSVGEENALMYETVQNLNPYLDENRPRYLMGVGTPEDLVENVERGVDMFDCVMPTRNARNGTFFTSFGKFNIKKAEFINDHEAIDPACSCYTCRNFSRGYLNHLFKAKELTFFRLASLHNLHYYLELARKMREAILNNSFTQFKRNFYHLRGK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Campylobacter jejuni (strain RM1221)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.554 kDa
Sequence
MEFKLKHKDGMARVCEITTAHSTFLTPVFMPVGTVGAVKSLDANDMKNELDAKIILANTYHMYLRPTSKVVKDFGGLHGFTKFDRSFLTDSGGFQAFSLSKNSKHFNEGIEFKSHIDGSRHLFTPKSVLDAQYDFNSDIMMILDDLVALPATKERVKISVDRTILWAKEAITYHKNMQNKGIGIGQNIFGIIQGGTDYEERKRCALSLNEMPFDGLAIGGLSVGEENALMYETVQNLNPYLDENRPRYLMGVGTPEDLVENVERGVDMFDCVMPTRNARNGTFFTSFGKFNIKKAEFINDHEVIDPTCSCYTCRNFSRGYLNHLFKAKELTFFRLASLHNLHYYLELARKMREAILNNSFTQFKRNFYHLRGK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.402 kDa
Sequence
MEFKVEYKSANARACRIKTTHSEILTPAFMPVGTLAAIKSLDAIDMSEILDAKIILANTYHLYLRPSSKVIKQMGGLHGFSKFDRSFLTDSGGFQAFSLNKISKPDEEGIKFKSHIDGSLHYFTPKSVLDAQYDFNSDIMMILDDLVALPASKERIELSLKRTIKWAKEAIDYHKLKQNQGVGMGQNIFGIIQGGTDFEARRICSQALCEMDFDGLAIGGLSVGEENEVMYDTVEAMMPYVDNNRPRYLMGVGTPEDLVENVARGVDMFDCVMPTRNARNGTLFTSFGKFNIKKAEFITDHSPIDSKCSCYTCKNFSRAYLNHLFKAKELTFFRLASLHNLHYYLNLAKQMREAIIKNEFENFKKEFYRQRTC

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.472 kDa
Sequence
MSFEKLGEDGKARRGRLTFPRGVVETPAFMPVGTYGTVKGMLPRDIEEIGAHIILGNTFHLMLRPGTEVVKAHGDLHDFTQWQGPILTDSGGFQVFSLGEMRKITEQGVTFRSPVDGSKVELSPEIAIQVQRDLGSDIVMIFDECTPYPATEKQAKESMELSLRWAERSKRAHEGNPAALFGIVQGGMYESLRDQSLEGLEKIGFDGYAIGGLSVGEPKEDMIRILDHLPPKMPEDKPRYLMGVGRPEDIVEAVRRGVDMFDCVMPTRNARNGYLFTSAGIVKIRNAKNRHDTGPLDERCDCYTCKHFSKSYLHHLDKCGEMLGSQLNTIHNLRFYQNLMSGLRGAIEAGTLSDFVSEFYALRGETVPPLGDS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.525 kDa
Sequence
MPAVTFTVLKRDRSTGARLGRLTTPHGTIETPVFMPVGTQATVKTMTPEEVAGLGAEIILANTYHLYLRPGADIIREAGGLHRFMHWERPILTDSGGFQVFSLADLREISDEGVTFRSHLDGSIHFLGPAESMAVQEALGSDIAMAFDECVAYPASPEEVAAGVERTSRWAEACLRAHRREDQAVFGIIQGGTIPELRRRSAREITALDFPGYGIGGLSVGEPKELMYSILEELQGYLPENKPRYLMGVGSPDCLIEGVKRGVDMFDCVLPTRIARNGTVMTTYGKLVVRNAAYARDFRPLDPECDCYTCRNYTRAYIRHLLKAEEILGLRLTTIHNLHFLIKLMQRLRQAIAEGRLEEVAADFYERYNSGKI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Sulfurovum sp. (strain NBC37-1)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.321 kDa
Sequence
MHFQIDKTDSKARACTIKTAHSTIQTPVFMPVGTVGAVKALDATDLATFIKPEIILGNTYHLYIRPGDEVIKTMGKLHGFTKYPKSFLTDSGGFQAFSLSDNVKIDEGGITFRSHLDGSKHYFTPKKVIDIQNNLGSDIMMILDDLVALPATQERIKASIERTTRWAEESITYHRANQKKGIGVDQNIFAIIQGGTDKAFREKSAKELCRLDYDGFAIGGLSVGEANQDMYDTVEWTTQFMPEEKPRYLMGVGTPEDLVENVSRGVDMFDCVMPTRNARNGTLFTSFGKVNIKKAEYTTDAGPIDPECGCMVCQTYSRAYLRHLFRSREITYFRLATIHNLYYYLNLMKEMREAILEERFNDFKVTFYRKRGK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.122 kDa
Sequence
MDFRIIARDASCHARRGRLRTAHGTFDTPVFMPVGTQASVKSLSPDELEDLGAHIILGNTYHLLLRPGAERVARLGGLHRFMHWNRSILTDSGGFQVFSLARINRIEEDGVVFQSHIDGARHAITPETSMECQMQLGSDIAMCFDECTAYPVTYEYARESMLRTVRWAARSKEAHTLPEQSLFGIVQGGVFCDLRRDCLERLVETGFDGYALGSLSVGESKEEMLSVLEAVAPGLPAASPRYVMGVGTPEDLVEGVRCGVDMFDCVMPTRNARNGMLFTVRGGIQIKNSRYADDDRPIEEGCSCYTCRRFSRAYLRHLFLARELLAYRLNTLHNLHYYLGLMAAMREAIEANAFDRWRRSFYLDRENREPAEE

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Synechococcus sp. (strain WH8102)
Length
373 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.782 kDa
Sequence
MFGFEISAHCANTAARCGCFHTPHGPVHTPRFMPVGTLATVKGISTDQLARTGAQMVLSNTYHLHLQPGEEIVAAAGGLHGFMGWDGPMLTDSGGFQVFSLGDLNKIDDRGVVFRNPRDGRIIDMTPEHATQIQMALGADVAMAFDQCPPYPATENDVIDACRRTHAWLARCVEAHSRDNQALFGIVQGGCFPHLRRESARAVADFDLPGIAVGGVSVGEPVEEMHRIVRDVTPLLPTHKPRYLMGIGTLREMAVAVANGIDLFDCVLPTRLGRHGTALVGGERWNLRNARFRHDHTPLDPSCPCPTCSGGHTRAYLNHLIRSEELLGLTLLSLHNITHLLRFTTAMSQAIRDGCFSEDFAPWEPDSPAHHTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Prochlorococcus marinus (strain MIT 9301)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.453 kDa
Sequence
MFEFEITSDCINTGARTGIFHTPNGKVNTPKFMPVGTLATVKGISSKQLISTGSEMILSNTFHLHLQPGEKLVKASGGIHKFMNWPKPILTDSGGYQVFSLAKLNNISDEGVEFKNPRDGSHVFLSPEKVIKIQMDLGSDVAMAFDHCPPHTANENDIEDSLERTHSWLQKCVETHQKSNQALFGIVQGGKYPRLREYSAKYTSSFDLPGIAVGGVSVGEAVEEIHSVINYVPKFLPINKPRYLMGIGSLKEISLAVANGFDIFDCVLPTRLGRHGTAFFNDERLNLRNARFKNDFSPIDKTCKCETCKSYSRAYLHHLIRNDEILGLSLISLHNIAHLIRFTNAISTAIRDNCFTNDFAPWKTSSIAHHTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Prochlorococcus marinus (strain MIT 9215)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.5 kDa
Sequence
MFEFEITSNCSNTKARTGIFHTPNGKVNTPKFMPVGTMATVKGISSKQLTSTGSEMILSNTFHLHLQPGEKLVKESGGIHNFMNWSKPILTDSGGYQVFSLAKLNNISDKGVEFKNPRDGSHVFLSPEKVIKIQMDLGSDVAMAFDHCPPHTANENDIEDSLQRTHSWLEKCIETHQKSNQALFGIVQGGKYPRLREYSAKFTSSFDLPGIAVGGVSVGEAVEDIHSVINYVPKFLPINKPRYLMGIGSLREISLAVANGFDIFDCVLPTRLGRHGTAFLNDERLNLRNARFKNDFSPIDKTCKCETCKSYSRAYLHHLIRNDEILGLTLISLHNIAHLLRFTNAISTAIKDNCFTNDFAPWKTSSIAHHTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Prochlorococcus marinus (strain MIT 9303)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.042 kDa
Sequence
MFDFQINAHCSHTRARVGCFRTPHGSVNTPRFMPVGTLATVKGITATQLADTGAQMVLANTYHLHLQPGEGIVADAGGLHRFMGWDRPLLTDSGGFQIFSLADLNRIDDHGVVFRNPRNGSQIELTPERAIEIQMALGADVAMAFDQCPPYPASESDVEAACKRTHAWLERCSNTHQLTNQALFGIVQGGCFPHLREQSAQIVASFDLPGIAIGGVSVGEPVEDIHRIVRQVSPLLPQDRPRYLMGIGTLREIAIAVASGIDLFDCVLPTRLGRHGTALVAGERWNLRNARFREDHTPLDQSCTCTACRHHSRAYLHHLIRNEELLGLTLLSLHNLTQLIRFTSAISQAIQDDCFSEDFAPWQPDSAAHHTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Chlamydophila caviae (strain GPIC)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.186 kDa
Sequence
MALKFHVLHQSKKSRARVGKIETAHGIIDTPAFVPVATNGALKGVIDHSNIPLMFCNTYHLLVHPGTEAIAAMGGLHKFMNRNAPIITDSGGFQIFSLAYGSVAEEIKSRGKKKGSSSILEVNDEGVWFKSYRDGHKLFLSPEVSVQAQKDLGADIIIPLDELLPFHSDEKYFLSSCSRTYVWEKRSLDYHKKDPRHQSMYGVIHGGIDPEQRKIGCQFVEDHPFDGFAIGGSLGRNLQEMLPVVDVTTSYLSKDRPVHLLGIGDLPSIHATVGLGIDSFDSSYPTKAARHGLILSSQGPIKIANQAYANDLSSLDPECTCATCTSNISRAYLRHLFKVHEPNAAIWASIHNLHYMQEVMKNIREQILNDEI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Chlamydia felis (strain Fe/C-56)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.29 kDa
Sequence
MALKFHVIHQSKKSRARVGRIETDHGIIDTPAFVPVATNGALKGVVDHSNIPLMFCNTYHLLVHPGTESIAAMGGLHKFINRDAPIITDSGGFQIFSLAYGSVAEEIKSHGKKKGSSSILEITDEGVWFKSYRDGHKLFLSPEVSVQAQKDLGADIIIPLDELLPFHSDQQYFLSSCSRTYVWEKRSLDYHRNDPRHQSMYGVIHGGIDPEQRKIGCQFVEDHPFDGFAIGGSLGRNLNEMVPVVDITTSHLSKDRPVHLLGIGDLPSIQATVKFGIDSFDSSYPTKAARHGLILSSQGPIKIANQAYANDLSPIDPKCTCLTCSSNLSRAYLRHLFKVHEPNAGIWASIHNLHHMQEVMKNIRKQILNDEI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Chlamydia muridarum (strain MoPn / Nigg)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.016 kDa
Sequence
MALRFEILHQSKKSRARVGRIETEHGCIDTPAFVPVATNGALKGVLDHSNIPLMFCNTYHLIVHPGAEAVAAMGGLHQFIGRNAPIITDSGGFQIFSLAYGSVAEEIKSCGKKKGENSIIKINDEGVWFKSYRDGRKLFLSPEVSVQAQKHLGADIIIPLDELLPFHTDPAYFQQSSQRTYAWEKRSLDYHLANPGYQSMYGVIHGGTFPDQRKLGCQFVEDLPFDGSAIGGSLGKNLRDIVGVVDVTTANLSIERPRHLLGIGDLPSIWATVGFGIDSFDSSYPTKAARHGMILTSQGSLKINNQRYASDLNPIEPGCACPACSQGISRAYLRHLFKVHEPNAGIWASIHNMHYMQKIMSKIREKILNDQL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Chlamydia pneumoniae
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.293 kDa
Sequence
MALKFHLIHQSKKSQARVGQIETSHGVIDTPAFVPVATHGALKGVIDHSDIPLLFCNTYHLLLHPGPEAVAKLGGLHQFMGRQAPIITDSGGFQIFSLAYGSVAEEIKSCGKKKGMSSLVKITDEGAWFKSYRDGRKLFLSPELSVQAQKDLGADIIIPLDELLPFHTDQEYFLTSCSRTYVWEKRSLEYHRKDPRHQSMYGVIHGGLDPEQRRIGVRFVEDEPFDGSAIGGSLGRNLQEMSEVVKITTSFLSKERPVHLLGIGDLPSIYAMVGFGIDSFDSSYPTKAARHGLILSKAGPIKIGQQKYSQDSSTIDPSCSCLTCLSGISRAYLRHLFKVREPNAAIWASIHNLHHMQQVMKEIREAILKDEI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.906 kDa
Sequence
MALRFEILHQSKKSRARVGRIETAHGYIDTPAFVPVATNGALKGVLDHSNIPLMFCNTYHLIVHPGAEAIAAMGGLHQFIGRNAPIITDSGGFQIFSLAYGSVAEEIKSCGKKKGGNTIIKVNDDGVHFKSYRDGRKLFLSPEISVQAQKDLGADIILPLDELLPFHADPTYFHQSSQRTYVWEKRSLDYHLKNPGIQSMYGVIHGGTFPDQRKLGCKFVEDLPFDGSAIGGSLGKNLQDIVEVVGVTAANLSAERPRHLLGIGDLPSIWATVGFGIDSFDSSYPTKAARHGMILTSQGPLKINNQRYSSDLNPIEPGCSCLACSQGITRAYLRHLFKVHEPNAGIWASIHNMHHMQKVMREIREGILNDRI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.932 kDa
Sequence
MALRFEILHQSKKSRARVGRIETAHGYIDTPAFVPVATNGALKGVLDHSNIPLMFCNTYHLIVHPGAEAIAAMGGLHQFIGRNAPIITDSGGFQIFSLAYGSVAEEIKSCGKKKGGNTIIKVNDDGVHFKSYRDGRKLFLSPEISVQAQKDLGADIILPLDELLPFHADPTYFHQSSQRTYVWEKRSLDYHLKNPGIQSMYGVIHGGTFPDQRKLGCKFVEDLPFDGSAIGGSLGKNLQDIVEVVGVTAANLSAERPRHLLGIGDLPSIWATVGFGIDSFDSSYPTKAARHGMILTLQGPLKINNQRYSSDLNPIEPGCSCLACSQGITRAYLRHLFKVHEPNAGIWASIHNMHHMQKVMREIREGILNDRI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.906 kDa
Sequence
MALRFEILHQSKKSRARVGRIETAHGYIDTPAFVPVATNGALKGVLDHSNIPLMFCNTYHLIVHPGAEAIAAMGGLHQFIGRNAPIITDSGGFQIFSLAYGSVAEEIKSCGKKKGGNTIIKVNDDGVHFKSYRDGRKLFLSPEISVQAQKDLGADIILPLDELLPFHADPTYFHQSSQRTYVWEKRSLDYHLKNPGIQSMYGVIHGGTFPDQRKLGCKFVEDLPFDGSAIGGSLGKNLQDIVEVVGVTAANLSAERPRHLLGIGDLPSIWATVGFGIDSFDSSYPTKAARHGMILTSQGPLKINNQRYSSDLNPIEPGCSCLACSQGITRAYLRHLFKVHEPNAGIWASIHNMHHMQKVMREIREGILNDRI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Chlamydia trachomatis (strain D/UW-3/Cx)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.906 kDa
Sequence
MALRFEILHQSKKSRARVGRIETAHGYIDTPAFVPVATNGALKGVLDHSNIPLMFCNTYHLIVHPGAEAIAAMGGLHQFIGRNAPIITDSGGFQIFSLAYGSVAEEIKSCGKKKGGNTIIKVNDDGVHFKSYRDGRKLFLSPEISVQAQKDLGADIILPLDELLPFHADPTYFHQSSQRTYVWEKRSLDYHLKNPGIQSMYGVIHGGTFPDQRKLGCKFVEDLPFDGSAIGGSLGKNLQDIVEVVGVTAANLSAERPRHLLGIGDLPSIWATVGFGIDSFDSSYPTKAARHGMILTSQGPLKINNQRYSSDLNPIEPGCSCLACSQGITRAYLRHLFKVHEPNAGIWASIHNMHHMQKVMREIREGILNDRI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.488 kDa
Sequence
MRFERLAQDGQARRGRLSFPRGTVETPAFMPVGTYGTVKGMTPQSVKDIGAEIILGNTFHLWLRPGTEVIETHGDLHDFAQWDKPILTDSGGFQVFSLGDMRKITEEGVHFRSPVDGAKVFMGPEESMAVQRSLGSDIVMIFDECTPYPATEAEAKRSMEMSLRWAERSRIAHGDSPSALFGIIQGGMYPELRERSLKGLLDIGFDGLAIGGLSVGEPKEEMLKVLDYLPGWMPDDKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGYLFTAEGTVKIRNAQHRYSTQALEADCDCHTCQHFSRSYLHHLDRCGEMLGAMLNTIHNLRYYQRVMAGLRTAIEAGTLTAFVEDFYARRGMPVPPLAA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.539 kDa
Sequence
MFRYELIGTDGGARRGVFHTPRGPVRTPGFMPVGTLGTVKGLTIDQVAATGADMILGNTYHLRLRPGHETVAALGGLHKMCGWDGPILTDSGGFQVFSLGAINKVNEHAATFRSHIDGAKIELTPEHSIEIQQALGSDVAMVLDHVIALPAPMTQVEDALARSIRWAARCRIAADREDQALFAIVQGGLDRTLRQQCASELAAMSFEGYAVGGLSVGEPPEDMYTTTGFTTPHLPADKPRYLMGVGTPRDLLENIARGIDLFDCVMPTRNGRNALAFTDEGPLKLRNAVHKLDTRPLMEDCPCLACRHSRGYLRHLFVAGEMLGPILLSHHNLMYYGRLMQATRDAIEAGEFEAFKNAKLAGWGHEPFQETV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Desulforudis audaxviator (strain MP104C)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.495 kDa
Sequence
MGILFEVLKQDSRTRARLGRLTTPHGVVETPVFMPVGTQATVKTMTPEEVRDLGARIILSNTYHLYLRPGHELVREAGGLHRFMHWNGPILTDSGGFQVFSLAPLRKLSDEGVEFRSHIDGSRHFFTPEKVVAVQEALGSDIAMVLDECAPYPCSYKDARTATERTTRWAARARAAWNSDGATALFGIIQGSVYRDLREESTRALVDLDFPGYGIGGLSVGEPKPLMYEALEWVIPLIPEDRPRYLMGVGSPDCLFEGIARGVDMFDCVLPTRMARHGAVFTHTGRLVVRNAPNARDFGPLDPGCTCYTCRHFSRAYVHHLLRAGEVLGIRLTTIHNLHFLLDLARRIREAIAEDRFHSLKEQFLAACLTPA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.966 kDa
Sequence
MAVRIEVLKEDNRTRARLGKLHTPHGVIETPVFMPVGTQATVKTMTPEELKDLGAGIILSNTYHLFLRPGHELIREAGGLHAFMHWDGAILTDSGGFQVFSLGDLRKITEEGVEFRSHLDGSKKFLSPEIATQVQMALGSDIVMAFDECTPYPATRDYAKASLERTTRWLKRCQETLTTTDRQALFGIVQGSMYEDLRKQSAAEITELDLPGYAVGGLSVGEPKELMYEVLDYTVPLLPKDKPRYLMGVGSPDALIEGVMRGIDMFDCVLPTRIARNGTALTRYGKLVVRNAESAHDFSPIDPTCDCYTCKNYSRAYLRHLIKADEILGLRLMTIHNLRFLTNLMSEIRAAIKENRLPEYREKFFYEYGYLK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.958 kDa
Sequence
MKFQIDKTDGNARACTITTAHSVIKTPIFMPVGTVGAVKSLDALDLKEILDAKIILANTYHMFLRPGSKIVKEFGGLHGFTKFDRSFLTDSGGFQAFSLRTNTKNDDDGIHFKSHIDGSLHYFTPTSVLDTQYDFGSDIMMILDDLVALPADPKRVKLSIERTIKWAKKAINYHLQKRESGVGLNQNIFGIIQGGTDENARKFCAQSLCELPFDGLAIGGLSVGETNREMYDTVEAVMPYIDSARPRYLMGVGTPEDIVENVERGVDMFDCVMPTRNARNGTLFTSFGKINIKSARFIHDDTPIDPCCDCYTCKNYSRGYLNHLYRAREITFYRLASLHNLHYYLHLVSDIRTAILEGKFLEFKKDFYSKRS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Chlamydia abortus (strain DSM 27085 / S26/3)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.256 kDa
Sequence
MALKFHVLHQSKKSRARVGRIETAHGIIDTPAFVPVATNGALKGVVDHSNIQLMFCNTYHLLVHPGTEAIAAMGGLHKFIHRNSPIITDSGGFQIFSLAYGSVAEEIKSCGKKKGSSSILEVTDEGVWFKSYRDGSKLFLSPEVSVQAQKDLGADIIIPLDELLPFHSDTTYFLSSCARTYVWEKRSLDYHKKDPRHQSMYGVIHGGIDPKQRKIGCAFVEDHPFDGFAIGGSLGRNLNEMVPIVDITTSYLSKDRPVHLLGIGDLPSIQATIGFGIDSFDSSYPTKAARHGLILSSQGPIKIANQAYTNDLSPIDPECTCLTCTSKISRAYLRHLFKVHEPNASIWASIHNLHYMQEFMKNIREQILHDRI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Prochlorococcus marinus (strain MIT 9211)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.177 kDa
Sequence
MFSFQINSNCSSTRARVGCLNTPHGDVHTPQFMPVGTLGTVKGVSPDQLLKTGSEMILANTYHLHLQPGEEIVHEAGGLHKFMGWDQPILTDSGGYQVFSLGKLNKIDDEGVEFKNPRDGSHLKLTPEIAIQIQMSLGSDIAMAFDQCPPYPATFNDVEEACLRTHNWLERSIAIHNKSDQALFGIIQGGCYPELREESARVVSSFNLPGIAIGGVSVGEPSDQINHIVRKVAPLLPEGIPRYLMGIGSLRELAIAVSNGIDLFDCVMPTRLGRHGTALVSGERWNLRNATFRNDHKPLDETCLCETCTNHTRAYLHHLIRSEELLGLTLLSVHNISHLIRFTRAMGRAIEDGCFSEDFAPWQKDSIAHYTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Prochlorococcus marinus (strain MIT 9515)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.656 kDa
Sequence
MFNFEVISSCSNTEARTGIFHTPHGQVRTPRFMPVGTLATVKGISSQQLKSTGSEMILSNTFHLHLQPGEKLIKEAGGIHEFMNWDKPVLTDSGGYQVFSLAKLNNITNEGVEFKNPRDGSPVFLSPDKVMRIQMDLGSDIAMAFDHCPPHTATENDIQDSLNRTHLWLENCVETHKKSNQALFGIVQGGRYPKLREISAKFTSSFGLPGIAVGGVSVGESVEQIHNVINFVPKFLPKDKPRYLMGIGSLKEITLAIAKGFDLFDCVLPTRLGRHGTAFFNDERWNIRNARFKNDFSPIDKTCKCETCKSYSRAYLHHLVRNDEILGLTLISLHNIAHLLRFTNAISAAIKDNCFTIDFAPWKRSSIAHHTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Prochlorococcus marinus (strain MIT 9312)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.58 kDa
Sequence
MFQFEITSNCSNTDARTGIFHTPNGQVNTPRFMPVGTLGTVKGISSKQLTSTGSEMILSNTFHLHLQPGEKLVKESGGIHKFMNWPKPILTDSGGYQVFSLAKLNNISDKGVEFKNPRDGSHVFLSPEKVMQIQMDLGSDVAMAFDHCPPHTANENDIEDSLLRTHSWLQKCVETHQKSNQALFGIIQGGKYPRLREYSAKFTSSFDLPGIAVGGVSVGEAVEEIHSVINYIPKFLPINKPRYLMGIGSLREISLAVAKGFDIFDCVLPTRLGRHGTAFFNDQRLNLRNARFKNDFSPIDKTCKCETCKSYSRAYLHHLIRNDEILGLTLISLHNIAHLIRFTNAISNAIKDNCFTIDFAPWKTASIAHHTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.346 kDa
Sequence
MFDFKVLSRSTNTAGRVGRLSTPHGILSTPQFMPVGTLGTVKGITATQLKDTNAQMILANTFHLHLQPGEAIIKESGGLHSFMSWDQPILTDSGGYQVFSLGKLNKIDDFGVSFKSPRDGSHIELTPEKAIQIQMDLGADVVMAFDQCPPYPASKVEVEEACKRTHLWLERCVATHSKEDQALFGIVQGGCFLDLREESARRVASFHLPGIAIGGVSVGEPSDQIHKIVRHVAPLLPNEVPRYLMGIGTIREMAVAVANGVDFFDCVLPTRLGRHGTALVRDERWNLRNACFRNDYQPLDTTCVCETCTNYNRAYLHHLIRNDELLGLTLLSLHNLSHLIRFSRAMAVAIEDDCFSEDFAPWQKSSIAHYTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Prochlorococcus marinus (strain MIT 9313)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.008 kDa
Sequence
MFDFQINAHCSHTRARVGCFRTPHGSVNTPRFMPVGTLATVKGITATQLADTGAQMVLANTYHLHLQPGEGIVADAGGLHRFMGWDRPLLTDSGGFQIFSLADLNRIDDHGVVFRNPRNGSQIELTPERAIEIQMALGADVAMAFDQCPPYPASESDVETACKRTHAWLERCSNTHQHANQALFGIVQGGCFPHLREQSAQIVASFGLPGIAIGGVSVGEPVEDIHRIVRQVSPLLPQDRPRYLMGIGTLREIAIAVASGIDLFDCVLPTRLGRHGTALVAGERWNLRNARFREDHTPLDQSCTCTACRHHSRAYLHHLIRNEELLGLTLLSLHNLTQLIRFTSAISQAIQDDCFSEDFAPWQPDSAAHHTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.711 kDa
Sequence
MFEFEIKSNCSNTEARTGIFHTPNGQVNTPRFMPVGTLATVKGISSEQLISTGSEMILSNTFHLHLQPGEKLVKESGGIHKFMNWDKPILTDSGGYQVFSLAKLNNISDKGVEFRNPRDGSHVFLSPEKVMQIQMDLGSDVAMAFDHCPPHTANENDIEDSLERTHSWLQKCVETHQKSNQALFGIVQGGKYPRLREHSAKFTSSFDLPGIAVGGVSVGEAVEEIHSVINNVPKFLPINKPRYLMGIGSLREISLAVAKGFDIFDCVLPTRLGRHGTAFFNDERWNIRNARFKNDFSPIDKTCKCETCKSYSRAYLHHLVRNDEILGLTLISLHNISHLIRFTNAISAAIKDNCFTIDFAPWKRSSIAHHTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Prochlorococcus marinus (strain AS9601)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.524 kDa
Sequence
MFEFEITSNCSNTAARTGIFHTPNGQVNTPKFMPVGTLATVKGISSKQLTSTGSEMILSNTFHLHLQPGEKLVKESGGIHKFMNWPKPILTDSGGYQVFSLAKLNNISDKGVEFKNPRDGSYVFLSPEKVIQIQMDLGSDVAMAFDHCPPHTANENDIEDSLQRTHSWLQKSVETHQKSNQALFGIVQGGKYPKLREYSAKYTSSFDLPGIAVGGVSVGETVEEIHSVINYVPKFLPIKKPRYLMGIGSLKEISLAVANGFDIFDCVLPTRLGRHGTAFFNDERLNLRNARFKNDFSPIDKTCKCETCKSYSRAYLHHLIRNDEILGLTLISLHNIAHLIRFTNAISTAIRDNCFTNDFAPWKTSSIAHHTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Pseudomonas aeruginosa (strain LESB58)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.205 kDa
Sequence
MNFELLATDGKARRGRLTFPRGVVETPAFMPVGTYGTVKGMLPRDIEDIGAQIILGNTFHLWLRPGTEVIQRHGDLHDFMQWKGPILTDSGGFQVFSLGAMRKIKEEGVTFASPVDGAKVFMGPEESMAVQRALGSDIVMIFDECTPYPADHDVAKRSMELSLRWAKRSKIAHGDSPSALFGIVQGGMHEDLRLRSLDGLQEIGFDGLAIGGLSVGEPKEEMIRVLDFLPPQMPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFVDSGVIKIRNSVHKHDDSTLDPTCDCYTCKHFSRAYLHHLDKCGEMLGSMLNTIHNLRHYQRVMAGLREAIQQGTLAAFVDAFYAKRGLPTPPLDA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.205 kDa
Sequence
MNFELLATDGKARRGRLTFPRGVVETPAFMPVGTYGTVKGMLPRDIEDIGAQIILGNTFHLWLRPGTEVIQRHGDLHDFMQWKGPILTDSGGFQVFSLGAMRKIKEEGVTFASPVDGAKVFMGPEESMAVQRALGSDIVMIFDECTPYPADHDVAKRSMELSLRWAKRSKIAHGDSPSALFGIVQGGMHEDLRLRSLDGLQEIGFDGLAIGGLSVGEPKEEMIRVLDFLPPQMPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFVDSGVIKIRNSVHKHDDSTLDPTCDCYTCKHFSRAYLHHLDKCGEMLGSMLNTIHNLRHYQRVMAGLREAIQQGTLAAFVDAFYAKRGLPTPPLDA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.205 kDa
Sequence
MNFELLATDGKARRGRLTFPRGVVETPAFMPVGTYGTVKGMLPRDIEDIGAQIILGNTFHLWLRPGTEVIQRHGDLHDFMQWKGPILTDSGGFQVFSLGAMRKIKEEGVTFASPVDGAKVFMGPEESMAVQRALGSDIVMIFDECTPYPADHDVAKRSMELSLRWAKRSKIAHGDSPSALFGIVQGGMHEDLRLRSLDGLQEIGFDGLAIGGLSVGEPKEEMIRVLDFLPPQMPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFVDSGVIKIRNSVHKHDDSTLDPTCDCYTCKHFSRAYLHHLDKCGEMLGSMLNTIHNLRHYQRVMAGLREAIQQGTLAAFVDAFYAKRGLPTPPLDA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.93 kDa
Sequence
MEFTLEATSKNARACTIKTAHSTIKTPVFMPVGTLGSVKALDMEDVLDLLGAEIILANTYHMYLRPGDETVAKMGKLHGFTTYPKSFLTDSGGFQAFSLSDISKASENGIEFRSHIDGSKHFFTPKKVIDIQHNLGSDIMMILDDLVALPATGERIALSIERTTAWAKESIEYFRKKQKEGIGAEQNIFAIIQGGTDKAFRTKSATELCALDFDGFAIGGLSVGELNNEMYDTVEHTVKYMPKDKPRYLMGVGTPEDLIENIERGIDMFDCVMPTRNARNGTLFTSFGRLNIKGATYKEDAQPVDSECECLTCKRYSRAYLNHLFRSREIAYFRLATIHNLHYYLNLMREAREAILEDKYAEFKAEFYRKRG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Synechococcus sp. (strain CC9311)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.034 kDa
Sequence
MFQFEIQATCSNTGARCGCFHTPHGPVTTPRFMPVGTLGTVKGVTTSQLAETGAQMVLSNTYHLHLQPGEEIVADAGGLHRFMGWDGPMLTDSGGFQVFSLGDLNRIDDEGVDFRNPRNGSRILLTPERSMQIQMRLGADVAMAFDQCPPYPATENDVAEACRRTHAWLGRCADAHQRDDQALFGIVQGGCFPHLRDLSARTVASFNLPGIAIGGVSVGEPVEEMHQIVRQVTPLLPADRPRYLMGIGTLREMAVAVANGIDMFDCVLPTRLGRHGTALVGGERWNLRNARFRHDHTPLDPNCPCIACRQHTRAYLHHLIRSEELLGLTLLSIHNLTHLIRFTTAMGQAIRDGCFSEDFAPWEPSSRAHHTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Synechococcus sp. (strain CC9902)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.924 kDa
Sequence
MFNFEISAHCPHTKGRCGCFHTPHGPVQTPRFMPVGTLATVKGISTEQLARTGAQMVLSNTYHLHLQPGEQVVAEAGGLHRFMGWDGPMLTDSGGFQVFSLGNLNKIDERGVVFRNPRDGRTIDMTPEHATNIQMALGADVAMAFDQCPPYPATENDVKDACRRTHAWLERCVNAHTRSDQALFGIVQGGCFPHLRRESARAVAAFDLPGIAIGGVSVGEPTDDMHRIVRDIGPLLPLDRPRYLMGIGTLREMAVAVANGIDLFDCVLPTRLGRHGTALVGGERWNLRNARFRNDHTPLDSSCSCLACTGHSRAYIHHLIRSDELLGLTLLSLHNITHLVRFTNAMAQAIQDGCFSEDFAPWQEDSPAHHTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Synechococcus sp. (strain CC9605)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.761 kDa
Sequence
MFGFEINAHCANTSARCGTFETPHGPVNTPRFMPVGTLATVKGISTEQLGRTGAQMVLSNTYHLHLQPGEEIVAAAGGLHRFMGWNGPMLTDSGGFQVFSLGDLNKIDDRGVVFRNPRDGRTIDMTPEHATQIQMALGADVAMAFDQCPPYPATENDVIDACRRTHAWLERCVTAHTREDQALFGIVQGGCFPHLRRESAMAVASFDLPGTAVGGVSVGEPAEEMHRIVRDVTPLLPSHKPRYLMGIGTLREMAIAVANGIDLFDCVLPTRLGRHGTVLVGGERWNLRNARFRHDHTPLDPSCSCVACTGHTRAYLHHLIRSEELLGLTLLSIHNITQLVRFTSAMAQAIRDGCFSEDFAPWEPDSPAHHTW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Brachyspira hyodysenteriae (strain ATCC 49526 / WA1)
Length
372 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.743 kDa
Sequence
MSFTFNVLKNSSQTSARLGKININGIEIDTPVFMPVGTKATVKALTPLMIEETESKIILANTYHLVLKPGLEVLKKFGGVKKFMNWKGAMLTDSGGFQVFSLAKLRKINDDGVEFSSHIDGSKYFFTPRSVMEAEHIIGADFIMCLDECSKHDASYDYVKEAMFRTHKWAKECKEYHDSTPNSEYQYLGGIIQGGMFDDLRKESAETLVNMDFPFYSIGGLSVGETPEQMHEVLSKVMLYTNKQKPRYLMGVSEPRDILNAVMEGIDMFDCVMPTRNARNGEAFTMNGIVRIRNSKYRMDDTVLEEDCDCYTCKNFSKAYLNHLDKTHEILFPILMTIHNVRFMQRFMKDLRNSIENDVFSDYRKDMMNKFY

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.313 kDa
Sequence
MKFQLHCRDHEARRGTLTLAHGTVETPAFMPVGTYGAVKGLSPDELHTLGAGIILGNTFHLWLRPGLEVIGAHGGLHRLMNWDGPILTDSGGFQVFSLGALRKICEEGVRFRSPVNGDTCFLTPEESMRIQQVLNSDIVMIFDECTPYPVDMQIAESSMQLSLRWAERSKTAHAGNPNALFGIVQGGMYESLRDHSAAGLCAIGFDGYAIGGLSVGEPKADMQRILRHTAPQLPADKPRYLMGVGTPEDIVHAVAQGIDLFDCVLPTRNARNGWLYTSQGILRLRNSRYRLDTSPPDEHCDCYTCRHFTRAYLHHLQRTGEMLGARLNSLHNLHYYQRLMANIRKAIETGQFEQFARKFSGQDFMLKCASV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.07 kDa
Sequence
MSIFQLLARDGAARRGTIRLPRGTVQTPAFMPVGTYGTVKAMSPEELKTLGAEIILGNTFHLFLRPGLEVISAVGGLHRMMHWDRPILTDSGGFQVFSLGALRKLTEAGVQFRAPTDGHMVFLGPEESMQIQAALGSDIAMVFDECTPHPASYEEARVSMELSLRWAARSHAAYAGPGELFGIVQGGMYADLRRRSLAGLQRLDFPGLAIGGLSVGESKVEMMQVLDDLMPHMPADRPRYLMGVGTPEDLVEGVRRGVDMFDCVMPTRNARNGWLFTRDGVLKLRNARYEKDVLPPDPACACYTCQNYSRAYLRHLQRSHEILGARLNTLHNLHYYQELMAGLREAIAAGRLDAYADDFYRRRRAGSLVGA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Acidithiobacillus ferrooxidans (strain ATCC 53993)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.07 kDa
Sequence
MSIFQLLARDGAARRGTIRLPRGTVQTPAFMPVGTYGTVKAMSPEELKTLGAEIILGNTFHLFLRPGLEVISAVGGLHRMMHWDRPILTDSGGFQVFSLGALRKLTEAGVQFRAPTDGHMVFLGPEESMQIQAALGSDIAMVFDECTPHPASYEEARVSMELSLRWAARSHAAYAGPGELFGIVQGGMYADLRRRSLAGLQRLDFPGLAIGGLSVGESKVEMMQVLDDLMPHMPADRPRYLMGVGTPEDLVEGVRRGVDMFDCVMPTRNARNGWLFTRDGVLKLRNARYEKDVLPPDPACACYTCQNYSRAYLRHLQRSHEILGARLNTLHNLHYYQELMAGLREAIAAGRLDAYADDFYRRRRAGSLVGA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.937 kDa
Sequence
MLKFTVHKTSGGARRGTLELNHGTVETPVFQPVGTYGSVKAMSPVELNDIGAQIILGNTFHLWLRPGLEIVEQFGGLHEFIGWDKPILTDSGGFQVFSLSDMRKLTEEGCTFQSPINGDKLFLSPEISMKIQTVLNSDIVMQLDECTPGQVDHATAQKSLQMSLRWAERSRRAFDDLKNPNALFGIVQGNLYTDLRQESLEGLMQVGFDGIAIGGLSVGEPKPEMYRMLTELKDMLPADKPHYLMGVGTPEDLVHGVANGVDMFDCVMPTRNARNGWIFTQWGDVKIKNARYKDDKKPLDEECACYACRNFSRAYLHHLHRVGEILGARLNTIHNLFYYQELMREMRKAIEEDRFEDFRLEFAAKRARSVN

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Helicobacter acinonychis (strain Sheeba)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.818 kDa
Sequence
MDFQLQAVDKHARAGILNLVHSQVETPIFMPVGTQGCIKSLDAIDMQERLSAKLILANTYHMYLRPGEKVIEQLGGLHHFAQFHGSFLTDSGGFQAFSLSDNVKLQEDGIVFKSHLDGSKHFFTPTKVLDIQYSLNSDIMMVLDDLVGLPAPLKRLEESIKRSAKWANISLEYHKENNRPNNNLFAIIQGGTHLKMRSLSVGLTHGGFDGYAIGGLAVGESTNEMLETIAHTAPLLPKDKPRYLMGVGTPENILDAISLGVDMFDCVMPTRNARNATLFTHSGKISIKNAPYKLDNTPIEENCTCYTCKRYSKAYLHHLFRAKELTYARLASLHNLHFYLELVKNARNAILEKRFLSFKKEFLERYTMDRQ

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Helicobacter pylori (strain P12)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.455 kDa
Sequence
MDFQLQATDKHARAGLLNLAHSQVATPVFMPVGTQGCIKSLDATDAQEILGAKLILANTYHMYLRPGEKAVGQLGGLHRFAQFQGSFLTDSGGFQAFSLSNNVKLQEDGIVFKSHIDGSKHLFTPIKVLDIQYSLNSDIMMVLDDLVGLPAPLKRLEESIKRSAKWANLSLEYHKEKNRPNNNLFAIIQGGTHLKMRSLSVGLTHKGFDGYAIGGLAVGESVDEMLETIAHTAPLLPKDKPRYLMGVGTPENILDAISLGVDMFDCVMPTRNARNATLFTHFGKISIKNAPYKLDDTPIEENCACYTCKRYSKAYLHHLFRAKELTYARLASLHNLHFYLELVKNARNAILEKRFLSFKKEFLEKYHSCSH

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Helicobacter pylori (strain G27)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.6 kDa
Sequence
MDFQLQAIDKHARAGLLNLAHSQVATPVFMPVGTQGCIKSLDAMDMQEILGAKLILANTYHMYLRPGEKVVEQLGGLHRFAQFHGSFLTDSGGFQAFSLSGNVKLQEDGIVFKSHIDGSKHFFTPAKVLDIQYSLNSDIMMVLDDLVGLPAPLKRLEESIKRSAKWANLSLEYHKEKNRPNNNLFAIIQGGTHLKMRSLSVELTHKGFDGYAIGGLAVGESVDEMLETIAHTAPLLPKDKPRYLMGVGTPENILDAISLGVDMFDCVMPTRNARNATLFTHSGKISIKNAPYKLDNTPIEENCACYACKRYSKAYLHHLFRAKELTYARLASLHNLHFYLEMVKNARNAILEKRFLSFKKEFLEKYHSCSH

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Helicobacter pylori (strain HPAG1)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.298 kDa
Sequence
MDFQLQAVDDNARAGLLNLAHSQVATPVFMPVGTQGCIKSLDATDAQEILGAKLILANTYHMYLRPGEKVVGQLGGLHRFAQFQGSFLTDSGGFQAFSLSGNIKLQEDGIVFKSHIDGSKHLFTPAKVLDIQYSLNSDIMMVLDDLVGLPAPLKRLEESIKRSAKWANLSLEYHKQKNRPSNNLFAIIQGGTHLKMRSLSVGLTHEGFDGYAIGGLAVGESVDEMLETIAHTAPLLPKDKPRYLMGVGTPENILDAIGLGVDMFDCVMPTRNARNATLFTYSGKISIKNAPYKLDNTPIEENCACYTCKRYSKAYLHHLFRAKELTYARLASLHNLHFYLELVKNARNAILEKRFLSFKKEFLEKYNSRSH

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Helicobacter pylori (strain J99 / ATCC 700824)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.507 kDa
Sequence
MDFQLQAVDDNARAGVLNLAHSQVETPVFMPVGTQGCIKSLDAMDAQEILGAKLILANTYHMYLRPGEKVVEQLGGLHRFAQFQGSFLTDSGGFQAFSLSDNVKLQEDGIVFKSHIDGSKHLFTPIKVLDIQYSLNSDIMMVLDDLVGLPAPLKRLEESIKRSAKWANMSLEYHKENNRPNNNLFAIIQGGTHLKMRSLSVGLTHEGFDGYAIGGLAVGESVDEMLETIAHTAPLLPKDKPRYLMGVGTPENILDAISLGVDMFDCVMPTRNARNATLFTHSGKISIKNAPYKLDDTPIEENCACYACKRYSKAYLHHLFRAKELTYARLASLHNLHFYLELVKNARNAILEKRFLSFKKEFLEKYHSCSH

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Helicobacter pylori (strain Shi470)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.391 kDa
Sequence
MDFQLQATDNNARAGLLNLAHSQVATPVFMPVGTQGCIKSLDATDMQGILGAKLILANTYHLYLRPGEKVVEELGGLHRFAQFHGSFLTDSGGFQAFSLSDNVKLQEDGIVFKSHIDGSKHLFTPAKVLDIQYSLNSDIMMVLDDLVGLPAPLKRLEESIKRSAKWANLSLEYHKQKNRPNNNLFAIIQGGTHLKMRSLSVGLTHEGFDGYAIGGLAVGESADEMLETIAHTAPLLPKDKPRYLMGVGTPENILDAIGLGVDMFDCVMPTRNARNATLFTHSGKISIKNAPYKLDDTPIEENCACYTCKRYSKAYLHHLFRAKELTYARLASLHNLHFYLELVKNARNAILEKRFLSFKKEFLKKYHSRSH

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Helicobacter pylori (strain ATCC 700392 / 26695)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.416 kDa
Sequence
MDFQLQATDNNARAGLLNLAHSQVATPVFMPVGTQGCIKSLDATDAQEILGAKLILANTYHMYLRPGEKVVEELGGLHRFAQFYGSFLTDSGGFQAFSLSDNVKLQEDGIVFKSHIDGSKHLFTPAKVLDIQYSLNSDIMMVLDDLVGLPAPLKRLEESIKRSAKWANMSLEYHKEKNRPSNNLFAIIQGGTHLKMRSLSVGLTHEGFDGYAIGGLAVGESADEMLETIAHTAPLLPKDKPRYLMGVGTPENILDAISLGVDMFDCVMPTRNARNATLFTHSGKISIKNAPYKLDNTPIEENCACYACKRYSKAYLHHLFRAKELTYARLASLHNLHFYLELVKNARNAILEKRFLSFKKEFLEKYNSRSH

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thioalkalivibrio sulfidiphilus (strain HL-EbGR7)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.546 kDa
Sequence
MKFELIANDGAARRGRLSFPRGTVETPAFMPVGTYGTVKAMTPEELEGIGAEIILGNTFHLMLRPGTEVIQLHGDLHDFMHWEKPILTDSGGFQVFSLADLRKITEEGVKFRSPVDGSEILLTPERSMDVQRALGSDIVMIFDECTPYPATEDQARESMELSLRWAARSKVAHGDSPSALFGIVQGGMYPALRSRSLEGLVDVGFDGYAIGGLSVGEGMEERHHVLDHLMPEMPAERPRYLMGVGKPEDIVEAVRRGVDMFDCVIPTRNARNGFLYTREGVMRIRNSRFRTDTGPIDESCDCYTCRNYSRAYLKHLDKCNEILGARLNTIHNLHYYQTLMRELRGAIAEGRLEAWVAEFYGRRSQAVPSVP

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.394 kDa
Sequence
MTFELLATDGKARRGRLTFPRGVVETPAFMPVGTYGTVKGMLPRDIEAIGAQIILGNTFHLWLRPGTEVIRRHGDLHDFMQWHGPILTDSGGFQVFSLGALRKIREEGVYFASPVDGAKVFMGPEESMRVQRDLGSDVVMIFDECTPYPADEEVARRSMELSLRWAGRSKIAHEGNPAALFGIVQGGMHEDLRLRSLDGLEEIGFDGLAIGGLSVGEPKEEMIRVLDFLPPRLPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVDSGVLKIRNAVHRHDESPLDPACDCHTCKHFSRAYLHHLDKCGEMLGSMLNTIHNLRHYQRLMTGLREAIQQGKLAAFVDTFYARRGLPVPPLT

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Caulobacter vibrioides (strain ATCC 19089 / CB15)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.009 kDa
Sequence
MAAFPFEIEATDGKARTGVLKTPRGDIRTPAFMPVGTAATVKAMTVDQVKDTGADIILGNTYHLMLRPSAERVKRLGGLHKFMRWDKPILTDSGGFQVMSLSGISKLTEEAVTFSSHVDGSKHVLTPERSIEIQADLLGSDIVMQLDECVAWPAEEARARKGMELSARWAKRSKDAFGTRDTQVLFGIQQGSTFENLRRESSERLREIGFDGYAIGGLAVGEGHQAMCEVLDYAPGFLPEDRPRYLMGVGKPIDLVEAVARGVDMFDCVLPTRSGRHGQAWTWDGPINLKNAKYAEDETPLDPDSDCPASRDYSKAYLRHLFKAEEILGQVLLSWHNIAFFQALTAAMRAAIAEGRFEQFRRDFAARHLGG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.336 kDa
Sequence
MSFELLATDGKARRGRITFPRGTVETPAFMPVGTYGTVKGMLPRDIEAIGAEMILGNTFHLWLRPGTEVIKKHNGLHDFMQWKGPILTDSGGFQVFSLGAMRKIKEEGVTFASPVDGSKVFMGPEESMQVQRDLGSDVVMIFDECTPYPAEHDVARTSMELSLRWAQRSKNAHADNTAALFGIVQGGMYQDLRMRSLEGLENIGFDGLAIGGLSVGEPKHEMIKVLDYLPDQMPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFVDTGVIKIRNAFHRHDESPLDPTCDCYTCTNFSRAYLHHLDKCGEMLSSMLNTIHNLRHYQRLMAGLREAIQQGKLAAFVDAFYAKRGLPVPPLD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.978 kDa
Sequence
MSFELLATDGKARRGRLTFPRGVVETPAFMPVGTYGTVKGMLPRDIEATGAQMILGNTFHLWLRPGTEVIKGHGDLHDFMQWKGPILTDSGGFQVFSLGAMRKIKEEGVTFASPVDGAKVFMGPEESMQVQRDLGSDVVMIFDECTPYPADEDVARVSMELSLRWAKRSKVAHGENTAALFGIVQGGMHENLRKRSLEGLDEIGFDGLAIGGLSVGEPKHEMIKVLDYLPGLMPADKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFIDTGVLKIRNAFHRHDNTPLDPTCDCYTCKNFSRAYLHHLDKCGEMLGSMLNTIHNLRHYQLLMAGLREAIQQGTLAAFVDAFYAKRGLPTPPLG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.962 kDa
Sequence
MLKFTLHKKDGLARRGTLELNHGKIETPVFMPVGTYGSVKAMNPQNLHDIKAQIILGNTYHLWLRPGLEVVEQFGGLHGFIGWDKPILTDSGGFQVFSLSDMRKLTEEGCTFKSPINGDKLFLSPEISMKIQTVLNSDIAMQLDECTPGETTREQARKSLQMSLRWAERSKKAFEDLKNPNALFGIVQGAMYEDLREESLRGLEEFDFPGLAVGGLSVGEPKPEMYRMLHAVGPMLPERKPHYLMGVGTPEDLVYGVAHGIDMFDCVMPTRNARNGWLFTRFGDLKIKNAKHKPDKRPIDESCTCYACQNFSRAYLHHLHRAGEILGAQLNTIHNLHFYQVIMAEMRDAVEQGKFADWQAQFHENRARGVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Neisseria gonorrhoeae (strain NCCP11945)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.955 kDa
Sequence
MLKFTLHKKDGLARRGTLELNHGKIETPVFMPVGTYGSVKAMNPQNLHDIKAQIILGNTYHLWLRPGLEVVEQFGGLHGFIGWDKPILTDSGGFQVFSLSDMRKLTEEGCTFKSPINGDKLFLSPEISMKIQTVLNSDIAMQLDECTPGETTREQARKSLQMSLRWAERSKKAFEDLKNPNALFGIVQGAMYEDLREESLRGLEEFDFPGLAVGGLSVGEPKPEMYRMLHAVGPILPEHKPHYLMGVGTPEDLVYGVAHGIDMFDCVMPTRNARNGWLFTRFGDLKIKNAKHKLDKRPIDESCTCYACQNFSRAYLHHLHRAGEILGAQLNTIHNLHFYQVIMAEMREAVEQGKFADWQAQFHENRARGVD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Neisseria meningitidis serogroup C (strain 053442)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.937 kDa
Sequence
MLKFTLHKKDGYARRGTLELNHGKIETPVFMPVGTYGSVKAMNPQNLHDIKAQIILGNTYHLWLRPGLEVIGQFGGLHGFIGWDKPILTDSGGFQVFSLSDMRKLTEEGCTFKSPINGDKLFLSPEISMKIQTVLNSDIAMQLDECTPGEATREQARKSLQMSLRWAERSKKAFEDLKNPNALFGIVQGAMYEDLREESLRGLEQFDFPGLAVGGLSVGEPKPEMYRMLRAVGPILPEHKPHYLMGVGTPEDLVYGVAHGIDMFDCVMPTRNARNGWLFTRFGDLKIKNAKHKLDKRPIDESCTCYACQNFSRAYLHHLHRAGEILGAQLNTIHNLHFYQVIMAEMRDAIEQGKFADWQAQFHENRARGTD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.934 kDa
Sequence
MLKFTLHKKDGYARRGTLELNHGKIETPVFMPVGTYGSVKAMNPQNLHDIKAQIILGNTYHLWLRPGLEVVEQFGGLHGFIGWDKPILTDSGGFQVFSLSDMRKLTEEGCTFKSPINGDKLFLSPEISMKIQTVLNSDIAMQLDECTPGEATREQARKSLQMSLRWAERSKKAFEDLKNPNALFGIVQGAMYEDLREESLKGLEELDFPGLAIGGLSVGEPKPEMYRMLRAVGPILPEHKPHYLMGVGTPEDLVYGVAHGVDMFDCVMPTRNARNGWLFTRFGDLKIKNAKHKLDKRPIDESCTCYACQNFSRAYLHHLHRAGEILGAQLNTIHNLHFYQVIMAEMREAVEQGKFADWQAQFHENRARGTD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Neisseria meningitidis serogroup B (strain MC58)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.945 kDa
Sequence
MLKFTLHKKDGLARRGTLELNHGKIETPVFMPVGTYGSVKAMNPQNLHDIKAQIILGNTYHLWLRPGLEVIGQFGGLHGFIGWDKPILTDSGGFQVFSLSDMRKLTEEGCTFKSPINGDKLFLSPEISMKIQTVLNSDIAMQLDECTPGEATREQARKSLQMSLRWAERSKKAFEDLKNPNALFGIVQGAMYEDLREESLRGLEQFDFPGLAVGGLSVGEPKPEMYRMLRAVGPILPEHKPHYLMGVGTPEDLVYGVAHGIDMFDCVMPTRNARNGWLFTRFGDLKIKNAKHKLDKRPIDESCTCYACQNFSRAYLHHLHRTGEILGAQLNTIHNLHFYQVIMAEMREAVEQGKFADWQARFHENRARGTD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.025 kDa
Sequence
MLKFTLHKKDGYARRGTLELNHGKIETPVFMPVGTYGSVKAMNPQNLHDIKAQIILGNTYHLWLRPGLEVVEQFGGLHGFIGWDKPILTDSGGFQVFSLSDMRKLTEEGCTFKSPINGDKLFLSPEISMKIQTVLNSDIAMQLDECTPGEATREQAKKSLQMSLRWAERSKKAFEDLKNPNALFGIVQGAMYEDLREESLRGLEQFDFPGLAVGGLSVGEPKPEMYRMLRAVGPILPEHKPHYLMGVGTPEDLVYGVAHGIDMFDCVMPTRNARNGWLFTRFGDLKIKNAKHKLDKRPIDESCTCYACQNFSRAYLHHLHRTGEILGAQLNTIHNLHFYQVIMAEMREAVEQGKFADWQARFHENRARGTD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Lawsonia intracellularis (strain PHE/MN1-00)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.438 kDa
Sequence
MNPPGTFHITATDGSARTGVLYTAHGIVNTPIFMPVGTVGSVKAIAPDDLEAISAEIILGNTYHLYLRPGDELIARRGGLHVFNAWEKPILTDSGGFQIFSLSSLRKLHKDGVIFRSHIDGSKHVFTPERVITIQRNLNSDIMMVLDECVAANADYTYTAQSLDLTIHWAKRSRDVYPKGEGDNLLFGIVQGGMFKSLRHSSVSQLIDLDFDGYAIGGLSVGEPKEIMMELLYDTAPLLPKTKPRYLMGVGTPLDILKGIEAGVDMFDCVLPTRNARNGTLYTSQGKLNIKRKEYAEDDLPLDENCSCYTCQTFSRAYLRHLFHSQELLAFRLNSIHNLTYFLNIIFGARKAIHGGYFFNYKQQVEQLYCN

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.98 kDa
Sequence
MSSIFKEGIYDTGSYARTGTLDLNGIQIQTPIFMPVGTRGSIKSLTSEDIDELGYNLILANTYHLYLKPGKEVFDHFQGLKNFMSYKKALLTDSGGFQVFSLASLFKFEDDGVRFQSHIDGSHHKFTPASVIDMQRSIGSDIMMVLDDCAPYGSDTKRLELALDRTHRWAKESFAYWMENPGGQNVFPIVQGGVNETLRLRSLETLQKIDFPGIAIGGLSVGEPRPEYIRILECMAPHLDKSRPRYLMGVGTVVDILEGVKNGIDMFDCVLPTRNARNGQVFTSKGKINLRNESHRLSDSPIDPQCECKVCKTYSLGYIRHLHKVKELTAFSLSTYHNLFFMQSFMEKMRKSIEIGNFQGFYDHWKNLFGS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
Length
371 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.98 kDa
Sequence
MSSIFKEGIYDTGSYARTGTLDLNGIQIQTPIFMPVGTRGSIKSLTSEDIDELGYNLILANTYHLYLKPGKEVFDHFQGLKNFMSYKKALLTDSGGFQVFSLASLFKFEDDGVRFQSHIDGSHHKFTPASVIDMQRSIGSDIMMVLDDCAPYGSDTKRLELALDRTHRWAKESFAYWMENPGGQNVFPIVQGGVNETLRLRSLETLQKIDFPGIAIGGLSVGEPRPEYIRILECMAPHLDKSRPRYLMGVGTVVDILEGVKNGIDMFDCVLPTRNARNGQVFTSKGKINLRNESHRLSDSPIDPQCECKVCKTYSLGYIRHLHKVKELTAFSLSTYHNLFFMQSFMEKMRKSIEIGNFQGFYDHWKNLFGS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.883 kDa
Sequence
MAVSFTITYKDESTGARLGLLYTPHGTVETPVFMPVGTQATVKTMTPEEVRDIGGRMILSNTYHLYLRPGHELIREAGGLHRFMHWDGPILTDSGGFQVFSLGPLRKVSEEGVAFRSHIDGSEHFFSPEKAMEVQMALGSDIAMAFDECAPYPCSREYALAATERTTRWARRCRTAHDREDQGLFGIVQGGTFKDLRERSARELVELDFPGYAIGGLSVGEPKQLMYEVLDYTVPLLPEEKPRYLMGVGSPDCLVEGVLRGIDMFDCVLPTRIARNGTALTRQGRLVVRNAEYARDFSPLEPDCDCYACRNYTRAYIRHLIKANEILGIRLTTIHNLYFIMKLMEEIRAAVRQGRMLQFRDDFLRKYQGD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.367 kDa
Sequence
MKYQLQKTDGRARLGKLIFERGLVDTPAFMPVGTYGSVKSMTPDEITETGAQIILGNTFHLWLRPGQDVIKLHGDLHDFMQWQGPILTDSGGFQVFSLNSMRKIEEKGVSFRHPLNGSEIFLSPEKSMEIQLDLGSDIVMVFDECPPYPSDLIYMKSSMEMSLRWANRSREHFNNLNNKNALFGIIQGGLSLELRETSLQGLLQIGFDGYAIGGLAVGEPKEEMYRVLDFLCPRIPDNKPRYLMGVGKPENLVEGVRRGIDMFDCVMPTRNARNGHLFVTHGVIKIRNTRYKTDISPLDPDCDCYTCRHYSRAYLHHLDRCNEILGARLNSIHNVRYYQRLMADLRHAIYEERLECFVEEFYKKIGLSIS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Hydrogenovibrio crunogenus (strain XCL-2)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.38 kDa
Sequence
MKFELDKQDGRARRGRLIFKRGVVETPAFMPVGTYGSVKGMMPEEVADTGAQIILGNTFHLSIRPGTDIIEQHGDLHDFMNWKGPILTDSGGFQVFSLGKMRKITEEGVHFRNPVNGSKIFMGPEESMDVQRKLGSDIVMIFDECTPYPATHDVAADSMRLSLRWAERSKQAHGDNPSALFGIVQGGMYEDLRQESIKGLTDIGFDGYAIGGLSVGEPKEEMMGTLDFTEPHMPKDKPRYMMGVGKPEDIVEAVRRGIDMFDCVIPTRNARNGFLFTHSGVVKIRNAVNKTSLEPLDAKCDCYTCQNYTRAYLHHLDKCGEIQGARLNTIHNLHYYQLLMKGLREAIASETLDTFVSEFYQARGEDVPAL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.121 kDa
Sequence
MKFELKNTNYLARRGKIIFDRGEVETPSFMPVGTYGSVKAMTPEELSSFGTQMILGNSFHLAITPGIDVVQAHGNLHDFMHWKGPILTDSGGFQVFSLGETRKISEKGVDFRSPKDGAKIFMGPEESIQIQKKLGSDIVMIFDECTPYPADKKTVYKSMQLSLRWAQRSKNEHDRLNNKNALFGIVQGGMHEDLRIQSAATLVEIGFNGFAIGGLSVGESKEEMIKVLDYLPSQLPSDKLRYLMGVGTPKDLVEAVERGIDMFDCVMPTRNARNGYLFTSIGIVKIRNARYRLDTSVLDECCHCYTCQNYSKSYLHHLQRKNEILGARLNTIHNLYYYQYLMLQMRRAIESNKFSKFKKEFYQQQGHDTL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.833 kDa
Sequence
MLTFDIINQSLESRARTGRITTAHGVIETPIFMPVGTLGTVKAVSVEELKACQAQIILGNTYHLYLRPGCEVMAHMGGLHPFMNWDRPILTDSGGFQFFSLAKLAKFKDEGVSFQSHIDGSRHLFTPERAVEIQSILGSDIMMSLDWCMGYPATRKEAMGALEKTTQWAERGRNFWIEQGRVNNLFGIVQGGMFADLRSISARQLADLDFPGYAIGGLSVGEPTELMYEMADHTVPQLPLEKPKYVMGVGTPENLVELAGMGVDMFDCVMPSRNARNGQLFTSTGTMNISNAAFRLDESPLDAECSCYTCQNYSRAYLRHLYKSRELLAYRLNTIHNLHYYLDLMHQMRNAINQGRFMAFKQEFYRKRER

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Desulfotomaculum reducens (strain MI-1)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.118 kDa
Sequence
MPVKIKIEKKEKHTRARLGKLTTPHGEVETPIFMPVGTQATVKTMTPEEVKETGGRLVLSNTYHLYLRPGHDLVKEAGGLHKFMNWDGPILTDSGGFQVFSLGPLRTITEEGVEFRSHIDGSKHFFTPEKVMEIEQALGADIAMAFDECAPYPCEKEYAVAALERTTRWAERCKRVHKREDQALFGIIQGGVFPDLRERSAKELLAMDFPGYGIGGLSVGEPKELMYEVLDQLMPIMPEDKPRYLMGVGSPDCLIEGVVRGVDMFDCVLPTRIARNGTVFTHNGKLTVRNAEYARDFRPMDQQCDCYACRNYSRAYIRHLIKTDEILGIRLTTIHNLHFIQHLMQNIRQAIREDRLLEYREDFLKVFNAG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Aromatoleum aromaticum (strain EbN1)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.455 kDa
Sequence
MQFELLAQHGAARRGRLTLAHGTVDTPAFMPVGTYGTVKAMTPAALADTGAQICLGNTFHLWLRPGLDVVAAHGGLHRFMNWDRPILTDSGGFQVFSLGALRKISEEGVKFASPIDGAKLFLTPEESMRIQTVLNSDIAMIFDECTPHPATHDEAAKSMQLSLRWARRSRDEFDRLANPNALFGIVQGGMFEDLRDESLAALDAIGFSGYAIGGLSVGEPKEDMARILAHTAPRLPAGRPRYLMGVGTPEDIVAGVAAGIDMFDCVMPTRNARNGWLFTRYGDIKIKNATHKQDTRPLDPSCDCYTCRNFSRAYLHHLHRAGEILGSMLNTIHNLRYYQTLTAELRAAIAAGDLDSHAARFRADRSTGAC

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Azoarcus sp. (strain BH72)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.941 kDa
Sequence
MQFELLSTSAGARRGRLTLAHGAVETPVFMPVGTYGTVKAMTPAMLSDVGAQICLGNTFHLWLRPGLDIVGAHGGLHRFMGWDKPILTDSGGFQVFSLGALRKISEEGVKFASPIDGARLFLTPEISMQIQTVLNSDVVMIFDECTPYPATRDEAAKSMRLSRRWARRSRDEFDRLENANALFGIVQGGMYEDLRDESLGALQDIGFHGFAIGGLSVGEPKDDMARILAHTAPRLPADKPRYLMGVGTPEDIVDGIANGIDMFDCVMPTRNARNGWLFTRYGDLKIKNAVHKADTRPLDPSCSCYTCRNFSRSYLHHLHRAGEILGSMLNTVHNLHYYQTLTAELRDAIAADRFADYVTRFRSERATGAH

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.769 kDa
Sequence
MNFEVLYQDNNARCGVFNFNQEIIETPVFMPVGTYGAVKSISTEEIKNTGSRIILSNAFHLYFRPGLEIIKLHGNLHNFMNWSGPILTDSGGFQVFSLSRFCKVNEEGVIFQNHIDGKKTFLTPKISMKIQSDLGSNIVMIFDQCIEYNQNWEKTKNAMERSLYWAKKSRIYFDSYKNKNSLFGIIHGGIYPSLRDISLQELIKIDFDGYALGGLAVGEPKIEMYKLLDHICPQIPKNKPRYLMGVGKPEDLIEGVRRGVDMFDCVIPTRNARNGHLFVTNGVIKIRNKKYKKDLSCLDKTCVCYTCRYYSRSYLHHLDACNEILGARLNTIHNLHYYQTLMSNIRNSIKNNTFEQFSLNFYKQKNKIDF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.74 kDa
Sequence
MNFKVLYQDNNARCGVFNFNQEIIETPVFMPVGTYGAVKSISTEEIKNTGSRIILSNAFHLYFRPGLEIIKLHGNLHNFMNWSGPILTDSGGFQVFSLSRFCKVNEEGVIFQNHIDGKKTFLTPKISMKIQSDLGSNIVMIFDQCIEYNQNWEKTKNAMERSLYWAKKSRIYFDSYKNKNSLFGIIHGGIYPSLRDISLQELIKIDFDGYALGGLAVGEPKIEMYKLLDHICPQIPKNKPRYLMGVGKPEDLIEGVRRGVDMFDCVIPTRNARNGHLFVTNGVIKIRNKKYKKDLSCLDNTCVCYTCRYYSRSYLHHLDACNEILGARLNTIHNLHYYQTLMSNIRNSIKNNTFEQFSVNFYKQKNKIDF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.741 kDa
Sequence
MNFEVLYQDNNARCGVFNFNQEIIETPVFMPVGTYGAVKSISTEEIKNTGSRIILSNAFHLYFRPGLEIIKLHGNLHNFMNWSGPILTDSGGFQVFSLSRFCKINEEGVIFQNHIDGKKTFLTPKISMKIQSDLGSNIVMIFDQCIEYNQNWEKTKNAMERSLYWAKKSRIYFDSYKNKNSLFGIIHGGIYPSLRDISLQELIKIDFDGYALGGLAVGEPKIEMYKLLDHICPQIPKNKPRYLMGVGKPEDLIEGVRRGVDMFDCVIPTRNARNGHLFVTNGVIKIRNKKYKKDLSCLDNTCACYTCRYYSRSYLHHLDACNEILGARLNTIHNLHYYQTLMSNIRNSIKNNTFEQFSLNFYKQKNKIDF

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.572 kDa
Sequence
MQFELDNTDGKARRGRLKFDRGIVETPAFMPVGTYGTVKGMTPEELDETGAHICLGNTFHLMLRPGTEIIKQHGDLHDFMHWQKPILTDSGGFQVFSLGDLRKITEEGVTFRSPINGEKILLTPEKSMQVQRDLGSDIVMIFDECTPHPATESEARQSMELSLRWAKRSKAEHGDNPSALFGIIQGGMYEGLRDVSLKGLEDIGFDGYAIGGLSVGEPKEDMIRILDHTTDKIPAHKPRYLMGVGKPEDLVEGVRRGVDMFDCVMPTRNARNGHLFVTSGIVKIRNAAHKTDTSPLDDKCDCYTCKNYSRSYLHHLDKCNEILGARLNTIHNLRYYQRVMQGLRDAIAEQKLDEFVADFYAQKDMPVPAL

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.314 kDa
Sequence
MEFTLIKQDGAARRGTVSLAHGDVQTPAFMPVGTYGAVKSLSPVEVRDTGAHILLGNTFHLWLRPGLEVIGEFGGLHRFMGWNGPILTDSGGFQVWSLGDLRKITEEGVRFRSPINGDSCFLTPEESMRIQKVLNSDIVMIFDECTPYPATPADARDSMLLSLRWAARSKAAHQGNPNALFGIIQGGMYEDLRDESLAGLTEIGFDGYAIGGLSVGEPKEDMLRILAHTTPKMPQDKPRYLMGVGTPEDLVAAVSHGVDMFDCVMPTRNARNGWLFTRHGDIKLKNARHRKDTRPLDEHCQCYTCLNFSRAYLHHLHRSGEILGARLNTIHNLHYYQELMLGMRQAIEQGRFEAFATEFRQGRQMLQQSA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.654 kDa
Sequence
MAISYQLEQTSSESRARLGKLKTPRGEIQTPVFMPVGTQATVKTMTPEELKNLDAEIILGNTYHLHLRPGNDIVREADGLHKFMNWDRPILTDSGGFQVFSLGKLRQISEQGVEFRSHIDGSKLFMTPEKSIEIQEDLGSDIMMVFDECPPYPAEYDYVKESMDRTIRWSKRCLQHQKHPEKQALFGIVQGGMYPELRKESALKTTELDFPGYAVGGLSVGEPKEMMLEVLNTTIPYLPEEKPRYLMGVGTPDYIIEAVRMGIDMFDCVYPTRVARNGTAMTRFGNLTVRNAVFQRDFQPIEEDCDCYVCQNYSRAYLRHLIKANEILGFRLLTWHNLFFLIKLIKELRQAIADDNFLAWRDSFYKNYQN

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Baumannia cicadellinicola subsp. Homalodisca coagulata
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.684 kDa
Sequence
MKYQLLKNCAGARRGRIQFDRGVVETPAFMPVGTYGTVKSLTTEEVKDTGTQMILCNAFHLWLRSEQEIIKLHGDLHHFMHWYGPIITDSGGFQIFSISNLNKITEAGVYFRHPINGSAIFLSPEKSMEIQYDLGSDIVMVLDECTPYPVQWDEAKKSMVMSLRWSERSHKRFHELKNNNALFGIIQGGMYKDLRDLSVKKLIEIGFDGYAIGGLSVGEPKENMHHILAHICPQLPEDKPRYLMGVGKPEDLIEGWRRGIDMFDCVIPTRNARNGHLFVTNGVVKIRNAKYKYDITSLDIYCDCYTCCNYSRAYLHHLSRCNEILGARLNTIHNLRYYQRLMADLRDAIDTGTSQYFIEEFYNKTRNSYY

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Laribacter hongkongensis (strain HLHK9)
Length
370 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.442 kDa
Sequence
MLEFTLHKTSGHARRGTLRLNHGTIETPVFMPVGTYGAVKAMTPDRLDETGAQIILGNTFHLWLRPGLDVIGTFGGLHDFTGWHKPILTDSGGFQVFSLGDLRKITEEGVHFQSPINGDKLFLSPEKSMEIQTVLNSDIVMQLDECTPGQVDHATAKASMQMSLRWAERSRRAFDDYRNPNALFGIVQGNLYLDLREESLKGLTDIGFDGIAVGGLSVGEPKPEMYRVLREVGPMLPADKPHYLMGVGTPEDLVEGVANGIDMFDCVMPTRNARNGWLFTRWGDVKIKNARYKDDTRPLDEQCSCYTCRHFSRGYLHHLHRTGEITGAMLNTVHNLHYYQELMADMRAAIEADSFAGFQQEFHAQRARGA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NS-E)
Length
369 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.194 kDa
Sequence
MEFEVKKTSGKARVGVLKLPHGVVRTPVFMPVGTNANVKLLTPRDLEEAGAEIVLSNTFHLMLKPGVEIIRLHGGLHKFMGWKKPILTDSGGFQVFSLPKLKIDDEGVTFKSPIDGSKVFLSPEISMEVQIALGSDICMAFDHCPPPDADYEVVKEATERTYRWALRSKEAFKTENQVLFGIVQGGVYPDLRKKSALQITSIGFDGYAIGGLSIGEERSLTLEMTEITVEYLPEDRPRYFMGGGSPELILELVDRGVDMFDSVFPTRIARHGTALTWKGRLNLKASYNKRSLDPVDEQCGCYTCKNFTRSYIHHLIDRGEVLGQILLSLHNVSFMISFMDEVRRSIEEGTFREFKGKMIDVYSSGGVSV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995)
Length
369 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.429 kDa
Sequence
MEFEVKKTFGKARLGVMKLHHGAVETPVFMPVGTNASVKLLTPRDLEEAGAEIILSNTFHLMLKPGVEIIKLHRGLHNFMGWKRPILTDSGGFQVFSLPKIRIDDEGVVFRSPIDGSKVFLNPEISMEVQIALGSDICMVFDHCPVPDADYEEVKEATERTYRWALRSKKAFKTENQALFGIVQGGIYPDLRRESALQLTSIGFDGYAIGGLSIGEERSLTLEMTEVTVEFLPEDKPRYFMGGGSPELILELVDRGVDMFDSVFPTRIARHGTALTWNGKLNLKASYNKRSLEPVDERCGCYTCKNFTRSYIHHLFDRGEVLGQILLTIHNINFMISLMKEVRRSIESGTFKELKSKVVEVYSSGGVNV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thermotoga sp. (strain RQ2)
Length
369 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.456 kDa
Sequence
MEFEVKKTFGKARLGVMKLHHGAVETPVFMPVGTNANVKLLTPRDLEEAGAEIILSNTFHLMLKPGVEIIKLHRGLHNFMGWKRPILTDSGGFQVFSLPKIRIDDEGVVFRSPIDGSKVFLNPEISMEVQIALGSDICMVFDHCPVPDADYEEVKEATERTYRWALRSKKAFKTENQALFGIVQGGIYPDLRRESALQLTSIGFDGYAIGGLSIGEERSLTLEMTEVTVEFLPEDKPRYFMGGGSPELILELVDRGVDMFDSVFPTRIARHGTALTWNGKLNLKASYNKRSLEPVDERCGCYTCKNFTRSYIHHLFDRGEVLGQILLTIHNINFMISLMKEVRRSIESGTFKELKSKVVEVYSSGGVNV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Dichelobacter nodosus (strain VCS1703A)
Length
369 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.907 kDa
Sequence
MNYECMTQDGRARRGRIIFDNGQIVQTPVFMPVGTQATVKGLSPEELDALGAEIILGNTFHLMLRPGAEIIQAHGGLHQFMHWQKPILTDSGGFQVFSLAKIRKLTEEGARFRSPIDGREVFLTPEKSIAVQHALNSNIIMQLDECTPYPATYDEAANSMRMSLRWARRSQQAHGDHANHLFGIVQGGIYPDLRQESAQALVELDLPGYAIGGLAVGEPKDAREATLDAVLPFVPKNKPRYLMGVGKPADLVEGVRRGIDMFDCVMPSRNARNAYLFTRFGILKLRNSRYKEDLRPIDETCNCYTCQRYSRSYLHHLDKCNEILGARLNTIHNLYYYVHLMHEMRRAIEEHRFDDFARAFYAEQECGND

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Dechloromonas aromatica (strain RCB)
Length
369 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.004 kDa
Sequence
MQFDLLKTDGVARRGTLTLAHGVIQTPVFMPVGTYGTVKAMTPQSLNDIGAQICLGNTFHLWLRPGLEVIAAHKGLHDFMNWQKPILTDSGGFQVFSLGAMRKITEEGVKFSSPHDGAKLFLTPEISMQIQKVLNSDIVMIFDECTPYPATHEEAAKSMRMSMRWAQRSRDEHNKLENSNALFGIVQGGMHEDLRDESVAGLCDIGFDGMAIGGLSVGEPKEDMARILAHTAPQLPTHKPRYLMGVGTPEDLVYSVSAGIDMFDCVMPTRNARNGHLFTRFGDVKIKNARYKLDTGPLDSSCSCYTCTNFTRAYLHHLFRNGEILGGMLNTIHNLHFYQTIMAEMRTAIEVEHFTEWAAGFARDRSSGQ

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Length
369 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.429 kDa
Sequence
MEFEVKKTFGKARLGVMKLHHGAVETPVFMPVGTNASVKLLTPRDLEEAGAEIILSNTFHLMLKPGVEIIKLHRGLHNFMGWKRPILTDSGGFQVFSLPKIRIDDEGVVFRSPIDGSKVFLNPEISMEVQIALGSDICMVFDHCPVPDADYEEVKEATERTYRWALRSKKAFKTENQALFGIVQGGIYPDLRRESALQLTSIGFDGYAIGGLSIGEERSLTLEMTEVTVEFLPEDKPRYFMGGGSPELILELVDRGVDMFDSVFPTRIARHGTALTWNGKLNLKASYNKRSLEPVDERCGCYTCKNFTRSYIHHLFDRGEVLGQILLTIHNINFMISLMKEVRRSIESGTFKELKSKVVEVYSSGGVNV

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Francisella philomiragia subsp. philomiragia (strain ATCC 25017)
Length
368 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.743 kDa
Sequence
MTVMKFDLIKKEGKARRGKISFPRGDIQTPAFMPVGTYGAVKSLSPVELKEMGADIILGNTFHLWLRPGTEIIKKHGTLHDFNGWDKPILTDSGGFQVFSLGKMRKLTEEGVTFKSPINGSKVFLSPEISMQVQRDLGSDIVMCFDECTPYPATEKEAKDSMELSMRWAKRSKDAHGDNPSALFGIIQGGMYEHLRDESLKALKEIDFDGFAIGGLSVGEPKEDMIRILDHTAHQMPEDKPRYLMGVGTPKDLVEAVYRGVDMFDCVMPSRNARNGHMFTSEGVVRIRNAKHKDDVSLLDPNCDCYTCQNFSRSYLHHLDKTQEILGSRLNTIHNLTYYQNLMKNIRQALEEGRFEEFRKEFLENYKG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Length
368 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
42.578 kDa
Sequence
MKFQVISQDKEARHGMFNFNGNIIETPVFMPVGTYGTVKSLNIEEIKNTGSKIILSNALHLYLRPGQDIIKLHGSLHNFMNWNGPILTDSGGFQIFSLSNFCRIKEEGVIFKNHINGKKFFLTPELSMEIQIDLGSNIIMIFDECIAYNKDWEKTKFAMERSLNWSRRSRIHFDLKKKNKKNLLFGIIHGGSYKSLRDISLKELIKMDFDGYALGGLAVGESKLEMHDLLDHITPQIPKKKPRYLMGVGKPEDLIESVYRGIDMFDCVLPTRNARNGHLFVTNGIIKIRNAKYKKDLSVLDKKCTCYTCQNYSRSYLHHLDSCNEILGARLNTIHNLHYYQTLMFNIRNAIKQKKFDEFVSNFYNQKK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Blochmannia pennsylvanicus (strain BPEN)
Length
368 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.983 kDa
Sequence
MPFQLLQTDGHARLGRLICNQGIVDTPAFMPVGTYGSIKTLTAKEVEASGTQIILSNTFHLWLRPGLDIIKLHGSLHKFMSWNGPIITDSGGFQVFSLSKTRTITRKGVGFKSPIDGHLVFLTPEKSIEIQHDLQSDIVMIFDECISYPNTWDYVKKSVNISLNWAERSRLRFDTLHNSNMLFAIIQGGMYENLRDMSAKELINIGFDGYAIGGLSVGEPKKEMYRILSHICKLIPTNKPRYLMGAGKPEDLLEAVQKGIDMFDCVIPTRNARNGYLFVSDGTIKIRNAQYKKDTSPLDGNCDCYTCQHYSRSYLHHLDCCKEILGVRLNTIHNLRYYQRLMEELRQAIKTKSLQNFIDIFYKRVNRI

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71)
Length
367 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.876 kDa
Sequence
MKFQLHRTDGLARRGTLSLTHGVVETPAFMPVGTYGAVKTMSPADLQVINAHIVLGNTFHLWLRPGLQVIEAHGGLHRFMGWDGPILTDSGGFQVFSLGVLRKITEQGVKFKSPVNGDTCFLTPEESMRIQYVLNSDIVMIFDECTPYPADERAVGESMELSLRWAERSRQAHDEGGNRNGLFGIVQGGMYEKLRDESLAGLLDIGFDGYAIGGLSVGEPKADMRRILRHTAPGLPAGKPRYLMGVGTPADIVDAVAQGMDMFDCVLPTRNARNGWLYTRTGVIKLRNSQYRLDTRPADEQCTCYTCRHFSRAYLHHLQRTGEILGARLNTLHNLYYYQQLMGEIRTAIENGQFQEYAQAFQAQTAS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Francisella tularensis subsp. tularensis (strain FSC 198)
Length
367 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.498 kDa
Sequence
MTVMKFDLIKKEGKARRGKITFPRGDIQTPAFMPVGTYGAVKSLSPVELKEMGAEIILGNTFHLWLRPGTEIIKKHGSLHGFNGWDKPILTDSGGFQVFSLGKMRKLTEEGVTFKSPINSSKVFLSPEISMQVQRDLGSDIVMCFDECTPYPATEKEAKESMELSMRWAKRSKEAHGDNPSALFGIIQGGMYEHLRDESLAKLKEIDFDGFAIGGLSVGEPKEDMIRILDHTAHQMPEDKPRYLMGVGTPKDLVEAVYRGVDMFDCVMPSRNARNGHIFTSEGVIKIRNSKYKDDTSPLDPNCDCYTCKNFTKSYLHHLDKTKEILGSRLNTIHNLTFYQNLMKSIRKALDEGRFSEFRKEFLASYK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA)
Length
367 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.484 kDa
Sequence
MTVMKFDLIKKEGKARRGKITFPRGDIQTPAFMPVGTYGAVKSLSPVELKEMGAEIILGNTFHLWLRPGTEIIKKHGSLHGFNGWDKPILTDSGGFQVFSLGKMRKLTEEGVTFKSPVNSSKVFLSPEISMQVQRDLGSDIVMCFDECTPYPATEKEAKESMELSMRWAKRSKEAHGDNPSALFGIIQGGMYEHLRDESLAKLKEIDFDGFAIGGLSVGEPKEDMIRILDHTAHQMPEDKPRYLMGVGTPKDLVEAVYRGVDMFDCVMPSRNARNGHIFTSEGVIKIRNSKYKDDTSPLDPNCDCYTCKNFTKSYLHHLDKTKEILGSRLNTIHNLTFYQNLMKSIRKALDEGRFSEFRKEFLASYK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Francisella tularensis subsp. holarctica (strain LVS)
Length
367 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.484 kDa
Sequence
MTVMKFDLIKKEGKARRGKITFPRGDIQTPAFMPVGTYGAVKSLSPVELKEMGAEIILGNTFHLWLRPGTEIIKKHGSLHGFNGWDKPILTDSGGFQVFSLGKMRKLTEEGVTFKSPVNSSKVFLSPEISMQVQRDLGSDIVMCFDECTPYPATEKEAKESMELSMRWAKRSKEAHGDNPSALFGIIQGGMYEHLRDESLAKLKEIDFDGFAIGGLSVGEPKEDMIRILDHTAHQMPEDKPRYLMGVGTPKDLVEAVYRGVDMFDCVMPSRNARNGHIFTSEGVIKIRNSKYKDDTSPLDPNCDCYTCKNFTKSYLHHLDKTKEILGSRLNTIHNLTFYQNLMKSIRKALDEGRFSEFRKEFLASYK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Francisella tularensis subsp. mediasiatica (strain FSC147)
Length
367 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.514 kDa
Sequence
MTVMKFDLIKKEGKARRGKITFPRGDIQTPAFMPVGTYGAVKSLSPVELKEMGAEIILGNTFHLWLRPGTEIIKKHGSLHGFNGWDKPILTDSGGFQVFSLGKMRKLTEEGVTFKSPINSSKVFLSPEISMQVQRDLGSDIVMCFDECTPYPATEKEAKESMELSMRWAKRSKEAHGDNPSALFGIIQGGMYEHLRDESLAKLKEIDFDGFAIGGLSVGEPKEDMIRILDHTAHQMPEDKPRYLMGVGTPKDLVEAVYRGVDMFDCVMPSRNARNGHIFTSEGVIKIRNSKYKDDTSLLDPNCDCYTCKNFTKSYLHHLDKTKEILGSRLNTIHNLTFYQNLMKSIRKALDEGRFSEFRKEFLASYK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Francisella tularensis subsp. novicida (strain U112)
Length
367 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.451 kDa
Sequence
MTVMKFDLIKKEGKARRGKISFPRGDIQTPAFMPVGTYGAVKSLSPVELKEMGAEIILGNTFHLWLRPGTEIIKKHGSLHGFNGWDKPILTDSGGFQVFSLGKMRKLTEEGVTFKSPINGSKVFLSPEISMQVQRDLGSDIVMCFDECTPYPATEKEAKESMELSMRWAKRSKDAHGDNPSALFGIIQGGMYEHLRDESLAKLKEIDFDGFAIGGLSVGEPKEDMIRILDHTAHQMPEDKPRYLMGVGTPKDLVEAVYRGVDMFDCVMPSRNARNGHIFTSEGVIKIRNSKYKDDTSPLDPNCDCYTCKNFTKSYLHHLDKTKEILGSRLNTIHNLTFYQNLMKSIRKALDEGRFAEFRKEFLANYK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Francisella tularensis subsp. holarctica (strain OSU18)
Length
367 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.484 kDa
Sequence
MTVMKFDLIKKEGKARRGKITFPRGDIQTPAFMPVGTYGAVKSLSPVELKEMGAEIILGNTFHLWLRPGTEIIKKHGSLHGFNGWDKPILTDSGGFQVFSLGKMRKLTEEGVTFKSPVNSSKVFLSPEISMQVQRDLGSDIVMCFDECTPYPATEKEAKESMELSMRWAKRSKEAHGDNPSALFGIIQGGMYEHLRDESLAKLKEIDFDGFAIGGLSVGEPKEDMIRILDHTAHQMPEDKPRYLMGVGTPKDLVEAVYRGVDMFDCVMPSRNARNGHIFTSEGVIKIRNSKYKDDTSPLDPNCDCYTCKNFTKSYLHHLDKTKEILGSRLNTIHNLTFYQNLMKSIRKALDEGRFSEFRKEFLASYK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Length
367 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.498 kDa
Sequence
MTVMKFDLIKKEGKARRGKITFPRGDIQTPAFMPVGTYGAVKSLSPVELKEMGAEIILGNTFHLWLRPGTEIIKKHGSLHGFNGWDKPILTDSGGFQVFSLGKMRKLTEEGVTFKSPINSSKVFLSPEISMQVQRDLGSDIVMCFDECTPYPATEKEAKESMELSMRWAKRSKEAHGDNPSALFGIIQGGMYEHLRDESLAKLKEIDFDGFAIGGLSVGEPKEDMIRILDHTAHQMPEDKPRYLMGVGTPKDLVEAVYRGVDMFDCVMPSRNARNGHIFTSEGVIKIRNSKYKDDTSPLDPNCDCYTCKNFTKSYLHHLDKTKEILGSRLNTIHNLTFYQNLMKSIRKALDEGRFSEFRKEFLASYK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Francisella tularensis subsp. tularensis (strain WY96-3418)
Length
367 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.498 kDa
Sequence
MTVMKFDLIKKEGKARRGKITFPRGDIQTPAFMPVGTYGAVKSLSPVELKEMGAEIILGNTFHLWLRPGTEIIKKHGSLHGFNGWDKPILTDSGGFQVFSLGKMRKLTEEGVTFKSPINSSKVFLSPEISMQVQRDLGSDIVMCFDECTPYPATEKEAKESMELSMRWAKRSKEAHGDNPSALFGIIQGGMYEHLRDESLAKLKEIDFDGFAIGGLSVGEPKEDMIRILDHTAHQMPEDKPRYLMGVGTPKDLVEAVYRGVDMFDCVMPSRNARNGHIFTSEGVIKIRNSKYKDDTSPLDPNCDCYTCKNFTKSYLHHLDKTKEILGSRLNTIHNLTFYQNLMKSIRKALDEGRFSEFRKEFLASYK

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thiobacillus denitrificans (strain ATCC 25259)
Length
367 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.855 kDa
Sequence
MKFDLLRTDGGARRGQLHLAHGVVQTPVFMPVGTYGTVKAMSPTEIADIGFEMLLSNTFHLWLRPGLEVIEAHGGLHRFMGWDKPILTDSGGFQVFSLGKLRKITEEGVKFASPTNGDKLFLTPETSMQIQRTLNSDIVMIFDECTPYPATERQAADSMRMSLRWAARSKAAHAGNPNALYGIVQGGMYEALRDESARELIGMDFDGYAIGGLSVGEPKDDMTRILAHTAPQLPADKPRYLMGVGTPSDLVAAVAAGIDQFDCVLPTRNARHGILFTRRGEIRIRNARWKLDTAPIDEECDCYACRHFTRAYVHHLIRAGEILGARLTTLHNLHYYHRLMAEVRAAIDAQRFSEFVARFHATQALGW

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thermosipho africanus (strain TCF52B)
Length
367 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.218 kDa
Sequence
MGLKFELLKTSGNARRGRIYLPHGVVETPTFMPVGTNANVKLMTPKLLDEIGAQIILGNAFHLYLKPGLDVFRFHGGIHNFMNWQKPVLTDSGGFQVFSLREGRKITEDGVLIRSPLDGSKHMITPELSMEIQHAIGSDIVMAFDYCAEPGISHQDAVVALELTSLWAERSLKKLRSLSDQAIFGIVQGAFFKDLRLRSAKEITSMNFDGFAIGGLSVGEEYDITLDMTKFTAPLLPENKPRYFMGAGSPKLIVDLVDSGIDMFDSVLPTRVARHGQALTWKGKLNIRSAKYKFSKEPIDESCGCYTCKNFSRSYIRHLFDRGEVLGQILLTIHNLHFMMDLSKKIRESIENDTFQELRGEVLKYYA

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429)
Length
367 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
41.571 kDa
Sequence
MALKFELLKTHKNARRGRIYLPHGVVETPTFMPVGTNANVKLMTPENLEEIGAQIILANAFHLYLKPGMEVLRHHNGIHDFMNWEKPILTDSGGFQVFSLRKGRKITKEGVLIKSPLDGSMRMITPELSMEIQNSIGSDIVMAFDYCAEPGISHQDAVVALELTTLWAERSLKSIRNMSDQSIFGIVQGAFYKDLRERSAKEITSMDFDGFAIGGLSVGEGYDITLEMTEFTVPLLPENKPRYFMGAGAPRLIVDLVNLGVDIFDSVLPTRVARHGQALTWKGKMNVRAAKYKFDKSPIDDECTCYTCRNYSRSYIRHLFDRGEVLGQMLLTIHNLHFMMDLSKKIRESIDGGYFEKLRGEVLKYYD

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Nitrosomonas eutropha (strain DSM 101675 / C91)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.596 kDa
Sequence
MKFQLHCHDHHARRGTLTLAHGMIETPAFMPVGTYGAVKGLSPDELQTLGAEIILGNTFHLWLRPGLEVIEAHGGLHRFMHWDGPILTDSGGFQVFSLGALRKISEEGVRFRSPVNGDTCFLTPEESMRIQRVLNSDIVMIFDECTPYPVDMQIAEDSMQLSLRWAERSKAAHAGNPNALFGIVQGGMYESLRDRSIAGLYNIGFDGYAIGGLSVGEPKLEMQRILSHTAPQLPVDKPRYLMGVGTPEDIVRAVEQGIDMFDCVLPTRNARNGWLYTSQGVLKLRNSRYRLDTSPPDENCDCYTCRHFTRAYLHHLQRTGEMLGARLNSLHNLHYYQRLMSDIRKAIEAGQFEQFACRFSG

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia africae (strain ESF-5)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.59 kDa
Sequence
MSKFSFNIHHQHKKARSGIIVTAHGEMRTPAFMPVGTRGTVKAMLPESVAETGADILLGNTYHLMLQPTAERIVQLGGLHKFMNWDKPILTDSGGFQVMSLSKLCKITEEGVSFSSHINGDKYMLTPERSTEIQYLLGSTITMAFDECTPYPATFEEAKTSMQLTTRWANRSRNAFVKREGYAQFGIIQGSVYEELREQSAKDLVELDFEGYAIGGLAVGEGQELMFKVLDYAPEFLPQNKPRYLMGVGKPVDIIGAVSRGIDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYADDNKPLEHDCLCPACRNYSKAYLHHLVRIGEILGSMLMTWHNLTYFQNLMSRIRAYIKLGKDFDFDS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia akari (strain Hartford)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.425 kDa
Sequence
MSKFSFNIHHQHKKARSGIIATAHGEIRTPAFMPVGTRGTVKAMLPESVAETGADILLGNTYHLMLQPSAERIARLGGLHKFMNWDKPILTDSGGFQVMSLSKLRKITEEGVSFSSHINGDKYMLTPERSTAIQYLLGSTITMAFDECTPYPVTFEEAKTSMQLTTRWAHRSRNAFVKREGYAQFGIIQGSVYEELREQSAKGLVELDFDGYAIGGLAVGEGQELMFKVLDYAPDFLPQNKPRYLMGVGKPADIIGAVNRGIDMFDCVIPTRSGRNGQAFTKYGTVNICNSKYSGDNEPLEHDCPCPACTNYTKAYLHHLVRIGEILGSMLMTWHNLTYFQNLISRIREYIKLGKDFDFYS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia bellii (strain OSU 85-389)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.373 kDa
Sequence
MSKFSFNINHQYKKARSGIITTAHGNIRTPAFMPVGTRGTVKAMLPESVAETGADILLGNTYHLMLQPSAERIAKLGGLHKFMNWGKPILTDSGGFQVMSLSKLRKITEEGVSFNSHINGDKYLLTPERSTEIQHLLGSTITMAFDECTPYPATFEEAKTSMQLTTRWAHRSREAFVKRDGYAQFGIIQGSTYEELREQSAKDLIELDFEGYAIGGLAVGEGQELMFKVLDYAPDFLPQNKPRYLMGVGKPADIIGAVSRGVDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYAEDNDPLEADCLCPACQNYSKAYLHHLVRIGEILGAMLMTWHNLTYFQNLMSRIREYIALGKDFDFTT

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia canadensis (strain McKiel)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.468 kDa
Sequence
MSKFSFNIHQMHKKARSGVITTAHGEIRTPAFMPVGTRGTIKAMLSESVAETGADILLGNTYHLMLQPSSERIARLGGLHKFMNWHKPILTDSGGFQVMSLSKLCKITEEGVSFSSHINGDKYMLTPERSTEIQYLLGSTITMAFDECTAYPATFEEAKTSVQLTTRWADRSRKAFVKREGYAQFGIIQGSVYQELREQSAKDLVKLDFEGYAIGGLAVGEGQELMFKVLDYTPNFLPQNKPCYLMGVGKPADIIGAVSRGIDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYADDDEPLEYDCLCPACKNYSKAYLHYLVKIGEILGSMLMTWHNLTYFQNLMSRIRTYIKAGQDFDFIT

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.59 kDa
Sequence
MSKFSFNIHHQHKKARSGIIVTAHGEMRTPAFMPVGTRGTVKAMLPESVAETGADILLGNTYHLMLQPTAERIVQLGGLHKFMNWDKPILTDSGGFQVMSLSKLCKITEEGVSFSSHINGDKYMLTPERSTEIQYLLGSTITMAFDECTPYPATFEEAKTSMQLTTRWANRSRNAFVKREGYAQFGIIQGSVYEELREQSAKDLVELDFEGYAIGGLAVGEGQELMFKVLDYAPEFLPQNKPRYLMGVGKPVDIIGAVSRGIDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYADDNKPLEHDCLCPACRNYSKAYLHHLVRIGEILGSMLMTWHNLTYFQNLMSRIRAYIKLGKDFDFDS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.592 kDa
Sequence
MSKFSFNIHHQHKKARNGVITTAHGEIRTPAFMPVGTRGTVKAMLPESVAETGADILLGNTYHLMLQPTAERIARLGGLHKFMNWDKPILTDSGGFQVMSLSKLRKITEEGVSFSSHINGDKYMLTPERSTEIQHLLGSTITMAFDECTPYPATFEEAKTSMQLTTRWANRSRNAFVKRDGYAQFGIIQGSVYEELREQSARDLVELDFEGYAIGGLAVGEGQELMFKVLDYAPDFLPQNKPCYLMGVGKPADIIGAVRRGIDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYADDNEPLEHDCLCPACKNYSKAYLHLLVRIGEILGAMLMTWHNLTYFQNLMSRIRKYIKLGKDFDFDS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia massiliae (strain Mtu5)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.628 kDa
Sequence
MSKFSFNIHHQHKKARSGIIVTAHGEMRTPAFMPVGTRGTVKAMLPESVAETGADILLGNTYHLMLQPTAERIVLLGGLHKFMNWDKPILTDSGGFQVMSLSKLRKITEEGVSFSSHINGDKYMLTPERSTEIQYLLGSTITMAFDECTPYPATFEEAKTSMQLTTRWANRSRNAFVKREGYAQFGIIQGSVYEELREQSAKDLVELDFEGYAIGGLAVGEGQELMFKVLDYAPDFLPQNKPRYLMGVGKPADIIGAVSRGIDMFDCVIPTRAGRNGQAFTKYGTVNIRNSKYADDNKPLEHDCLCPACRNYSKAYLHHLVRIGEILGSMLMTWHNLTYFQNLMSRIREYIKLGKDFDFDS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia prowazekii (strain Madrid E)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.785 kDa
Sequence
MSKFSFTIHSHYKKARSGVITTAHGEIRTPAFMPVGTRGAVKAMLTEAVVETGADILLGNTYHLMLQPSAERIAYLGGLHKFMNWDKPILTDSGGFQVMSLSKLCKITEEGVSFRSHINGNKYMLTPEYSTEIQYLLGSTITMALDECTPYPSTFEKAKTSMHLTTRWANRSRDAFVKREGYAQFGIIQGSVYKELREQSVKDLVKCDFEGYAIGGLAVGEGQELMFRVLDYVPDFLPQNKPRYLMGVGKPSDIIGAVSRGIDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYADDKEPLEHDCKCPACTNYTKAYLHHLVRIREILGPMLMTWHNLTYFQNLMSRIRTYIKLGKDFDFVH

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia peacockii (strain Rustic)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.576 kDa
Sequence
MSKFSFNIYHQHKKARSGIIVTAHGEMRTPAFMPVGTRGTVKAMLPESVAETGADILLGNTYHLMLQPTAERIVQLGGLHKFMNWDKPILTDSGGFQVMSLSKLCKITEEGVSFSSHINGDKYMLTPERSTEIQYLLGSTITMAFDECTPYPATFEEAKTSMQLTTRWANRSRNAFVKREGYAQFGIIQGSVYEELREQSSKDLVELDFEGYAVGGLAVGEGQELMFKVLDYAPDFLPQNKPRYLMGVGKPADIIGAVSRGIDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYADDNKPLEHDCLCPACRNYSKAYLHHLVRIGEILGSMLMTWHNLTYFQNLMSRIRAYIKLGKDFDFDS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia rickettsii (strain Iowa)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.563 kDa
Sequence
MSKFSFNIHHQHKKARSGIIVTAHGEMRTPAFMPVGTRGTVKAMLPESVAETGADILLGNTYHLMLQPTAERIVQLGGLHKFMNWDKPILTDSGGFQVMSLSKLCKITEEGVSFSSHINGDKYMLTPERSTEIQYLLGSTITMAFDECTPYPATFEEAKTSMQLTTRWANRSRNTFVKREGYAQFGIIQGSVYEELREQSAKDLVELDFDGYAIGGLAVGEGQELMFKVLDYAPDFLPQNKPRYLMGVGKPADIIGAVSRGIDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYADDNKPLEHDCLCPACRNYSKAYLHHLVRIGEILGSMLMTWHNLTYFQNLMSRIRAYIKLGKDFDFDS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia rickettsii (strain Sheila Smith)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.563 kDa
Sequence
MSKFSFNIHHQHKKARSGIIVTAHGEMRTPAFMPVGTRGTVKAMLPESVAETGADILLGNTYHLMLQPTAERIVQLGGLHKFMNWDKPILTDSGGFQVMSLSKLCKITEEGVSFSSHINGDKYMLTPERSTEIQYLLGSTITMAFDECTPYPATFEEAKTSMQLTTRWANRSRNTFVKREGYAQFGIIQGSVYEELREQSAKDLVELDFDGYAIGGLAVGEGQELMFKVLDYAPDFLPQNKPRYLMGVGKPADIIGAVSRGIDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYADDNKPLEHDCLCPACRNYSKAYLHHLVRIGEILGSMLMTWHNLTYFQNLMSRIRAYIKLGKDFDFDS

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia typhi (strain ATCC VR-144 / Wilmington)
Length
361 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.773 kDa
Sequence
MSKFSFTIHSNYKKARSGVITTAHGKIRTPTFMPVGTRGTVKAMLTESVVETGADILLGNTYHLMLQPSAERIAYLGGLHKFMNWDKPILTDSGGFQVMSLSKLRKITEEGVSFRSHINGNKYMLTPEYSTEIQYLLGSTITMALDECTPYPSTFEEAKTSMNLTTRWANRSRDAFVKREGYAQFGIIQGSVYKELREQSVKDLVKFDFDGYAIGGLAVGEGQELMFKVLDYVSDFLPQNKPRYLMGVGKPADIIGAVSRGIDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYAEDKAPLEYDCKCPACTNYTKAYLHHLVRIREILGPMLMTWHNLTYFQNLMSRIRAYIKLGKDFDFVN

Gene
tgt
Protein
Queuine tRNA-ribosyltransferase
Organism
Rickettsia bellii (strain RML369-C)
Length
359 amino acids
Function
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Similarity
Belongs to the queuine tRNA-ribosyltransferase family.
Mass
40.095 kDa
Sequence
MSKFSFNINHQYKKARSGIITTAHGNIRTPAFMPVGTRGTVKAMLPESVAETGADILLGNTYHLMLQPSAERIAKLGGLHKFMNWGKPILTDSGGFQVMSLSKLRKITEEGVSFNSHINGDKYLLTPERSTEIQHLLGSTITMAFDECTPYPATFEEAKTSMQLTTRWAHRSREAFVKRDGYAQFGIIQGSTYEELREQSAKDLIELDFEGYAIGGLAVGEGQELMFKVLAPDFLPQNKPRYLMGVGKPADIIGAVSRGVDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYAEDNDPLEADCLCPACQNYSKAYLHHLVRIGEILGAMLMTWHNLTYFQNLMSRIREYIALGKDFDFTT