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cbiA

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Length
497 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source (Potential). Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation (PubMed:27846569). Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source (PubMed:27846569).
Similarity
Belongs to the CobB/CbiA family.
Mass
53.485 kDa
Sequence
MSHSKQSGTEAGSIPRVLISADRSSSGKTTISMGLMAALVSRGYKVQPFKVALDYIDPSYHTEITGRFCRNLDGYLMDENGILDVYSHACETGSGADIAIIEGVRGLYEGFEGLSDLGSTAQIAKILKCPVVFVINARSITRSAAALISGYKNFDPDVEIAGVILNNIGGRRHAQKAKEAIEHYTGVPVIGIIPRDPSMQISMRHLGLMPALEGRRRLGDGGFEDRLRGIEEIINKGIDVDRFLEIAGSAKSLTSPENSIFSPAAGAGSPRPRIGIALDEAFNFYYRDNIDLLELAGAEIVYFSPVNDPELPDVDGLYIGGGYPELFAAELEANESMRRSIKEASAAGMPIYAECGGLMYLTEKISTGVPGKGTYHDASMPESTYIMVGALPGHTIMGQTRVVSYNIGTLDRDCLIGKEGNSFKGHEFHHSEIREIPEYAEFAIALLRGTGIKGDRDGLIVGNTLGSYAHLHGVAYRELAGSLVEAAGKFRASRAPR

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Methanosarcina barkeri (strain Fusaro / DSM 804)
Length
494 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source (Potential). Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation (PubMed:28225763). Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source (PubMed:28225763). Also able to use sirohydrochlorin as substrate, but only produces a monoamide species in a much slower reaction (PubMed:28225763). Unable to use other metallosirohydrochlorins such as sirohaem and Co-sirohydrochlorin (PubMed:28225763).
Similarity
Belongs to the CobB/CbiA family.
Mass
53.786 kDa
Sequence
MLNDKQSVENIPRILISADRSSSGKTTISMGLMAALVSRGYKVQPFKVALDYIDPSYHTEITGRFCRNLDGYLMDENGILDVYTHACEAGEKADIAIIEGVRGLYEGFESLSDLGSTAQIAKILNCPVIFVINARSITRSSAALINGYRNFDPDVEIAGVILNNIGSRRHAKKAKEAIEYYTGVPVIGIVPRDPAMQISMRHLGLMPALEGRRRLGDGGFEARLRGIEEIINKGIDVDRFMEIAKSAKALKSPENSVFSSVSDPGAPRPKIGVALDEAFNFYYRDNIDLLNLAGAEIVYFSPVKDASLPEVDGLYIGGGYPELFAAELEANESMRQDIKKASAAGMPIYAECGGLMYLTEKISTGVPGKGTYHDASMPESTYSMVGALPGHTIMGQTRVVSYNIGTLNKDCLLGKKYNSFKGHEFHHSEIREIPEDAEFAITLSRGTGIKNGMDGLISGNTLGSYAHLHGVAYREFASSLVEAARNFRDSRVLP

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
482 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
53.854 kDa
Sequence
MTVIIAGERSGAGKTTITLAMLAYLARQKLRVQSFKVGPDYIDPMFHSQITGRPCRNLDPFLTSEAYVQRCFHYHSQGTPYSLIEGVMGLFDGVPYQGLTDYSSTAHIARLLNLPIVFVMDCQRLSGSVAAIVQGYRHWQPGVNLVGVILNRVGGDRHLELLKIALEPLRIPILGVFFRQQDLTLPDRHLGLVPCGELPQIQQYFDQLAHVAAQQLDWPKLLPLLETPRNLPSPMSLFDVPQKSPQARLAIAQDQAFNFYYADNLDLLTHCGFELIPFSPLEDTELPPAIDGVYLGGGFPELFAEQLSQNQALKDQLKTLIHQGLPTYGECGGLMYLSQSLTNFEGQIFPMLEMLPTAVTMGGKLSLGYRQAQVVNSHSWLWQTESLRGHEFHRSQMTKLPNQALYRQRGLLAIDQNTTDGWCVGSVQASYLHLHWGSQISTVEKFRAACLAFQKKLSYLGKHPPFKSVPLRNTGGDAHGRE

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
Length
467 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
51.067 kDa
Sequence
MPYRIPRLFISATRKSSGKTFIAVGLTAALSARGLVVQPFKKGPDYIDPRWHSLAAGRECRNLDDFIMGRPKVLTSFVAHAQGADVAIIEGNLGLFDGQDLEGSDSSAALAKALGAPVLLVVDCKHLARSVAPLVCGHLHFPGGETIVGIILNNVATPRQEKRLREAIERFCPIPILGAIPRSAEIMIDERHLGLVPANEKQGAPHTVETMGRMMESHLDLDRLVALAATATPLALPDNPPALASKAPLVGGRPVRVGYAADQAFSFYYPDNLEALRQNGVELVPFSLLDEQPLPQVDGLYIGGGFPEMFMEHLQQNRATLETIRTRSELGMPIYAECGGLMVLSQRLIWAGKRVELAGALPIEITMHPKPQGYGYMKIHGTGALPWPPVDQEICCHEFHYSKVSKLGEGVRFAYQVTRGSGVDGWHDGILYHNIFASYAHIHVEGAPEWAPFLARFWRERGSFSQP

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1)
Length
463 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
48.879 kDa
Sequence
MSINGFLIAAPQSGSGKTTISLAIMAALRRRGLVVAPFKCGPDFIDPGYHRMASGRASINLDGWMCPESFVAETFRLHAEAADVAVIEAVMGLFDGLGASPLQGSSAQIAAICGAPVVLVVNARGMAASAAALVKGFAEFDPDVRLAGVIFNNVGSAGHAELLARVMASALPEIALLGCIPRDEALAIPSRHLGLVTAEDNPLPPEYLDRLADLAEKHLDLAGLAGLRITPRSVGASLSRTNGGGMLPVRIAVARDAAFCFVYQDNLRLLREAGGELLFFSPLADGALPEGISGIYLPGGYPELYAERLAVNVPMLDAIRGAARDGMPLYAECGGFIYLTRGMEDSQGAPLADFAGIFPVRARMLPKRKALGYRQVECLSVSILGPAGETARGHEFHYSEICEMPVDVTRTYSVTRQGAFLGQEGYCLSNCLASYVHLHFGSNPCLAPSLVAACRKFAATRRS

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Pelobacter carbinolicus (strain DSM 2380 / NBRC 103641 / GraBd1)
Length
459 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
49.296 kDa
Sequence
MSCPRLVIAGTSSGAGKTSLTLGLTAALRRRGLKVQTFKVGPDFLDPTWLSLASERPCINLDGWMCGERYVRDRFATATADADIAIVEGVMGLFDGADPAAAAGSTAEIARWLDAPVLLVVNAHGMARSLAALVKGYAEFDPDLHLAGVIANRCGSTRHGDWLSEALCAAGMPPLTGTVIRDSLPPLPSRHLGLVTADRQHLTSEALNTLADAVERQLDMPRILDLAEKVPATPGVAATASSTEGRPVRIGMAFDEAFHFYYPDNLQALEDAGATLVRFSPMHDDTLPADLDALLLGGGYPEEYADTLETNQTMRQAVADFAAADRPIYAECGGLMYLSEGIELRDGSRHAMTGALPFATRMLATRKRLGYAEVRHLAHGPFGPAGTCLRGHEFHYSEAIAEPAAPGWQSAWQVSYRRSNKPVAEGYQRGRLFASYVHTHFASRPGAARAFVDFCRGES

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
459 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Is able to use other nucleotide triphosphates as substrate, such as GTP or UTP, although less efficiently than ATP.
Similarity
Belongs to the CobB/CbiA family.
Mass
50.037 kDa
Sequence
MAARHHAFILAGTGSGCGKTTVTLGLLRLLQKRALRVQPFKVGPDYLDTGWHTAICGVASRNLDSFMLPPPVLNALFCEQMRQADIAVIEGVMGLYDGYGVDPNYCSTAAMAKQLGCPVILLVDGKAVSTSLAATVMGFQHFDPTLNLAGVIVNRVTSDAHYQLLKNAIEHYCSLPVLGYVPPCDGVALPERHLGLITARESLVNQQSWHDFAATLEQTVDVDALLSLSVLSALPAGMWPERPDNTAGAGLTLALADDEAFNFYYPDNIDLLERAGVNIVRFSPLHDRALPDCQMIWLGGGYPELYAADLAANTVMLKHLRAAHQRGVAIYAECGGLMYLGSTLEDSGGEIHQMANIIPGHSKMGKRLTRFGYCEAQAMQPTLLAAPGEIVRGHEFHYSDFIPETPAVMACRKVRDGRVLQEWTGGWQTGNTFASYLHVHFAQRPEMLQHWLAAARRVL

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Length
456 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
50.345 kDa
Sequence
MALIIAGERSGVGKTTTTLTLLAALKARQASVQSFKVGPDYIDPMFHRFVTGRDCRNLDPILTDEDYVQHCFQQHSQTADYTLVEGVMGLFDGLTGKTDTASTAHIARILNLPILLVLNCSSTARSIAAIAYGYQNFDSRLKIAGLVLNRVGSDRHLELLKDALEPLEIPILGVLRRQDEIQIPDRHLGLIPTSELPHLQSVIDRLAVLGQQCFDWNRLEPLLSNSDLNSTAFKSTTPSISLKSSVPIAIARDRAFNFYYADNFDLLRAAGAELIEWSPLQDRQLPAGVQGLYLGGGFPEVFAAELSDNLLARQAVQTAITQGIPCYAECGGLMYLRQHIIDFEQTQYPMVGAIAATAQMGSRLTLGYREATAQQASPLLQKGQVVWGHEFHRSSLREPIAQPLFQLQNFDGSLHYGEGYSQPNLHASYLHLHFGGKPWLIQNFLQACQQATALSR

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Lactobacillus reuteri (strain JCM 1112)
Length
454 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
50.775 kDa
Sequence
MKKVLIAGVTSGSGKTTAVLGILKALNEKYTIQSYKVGPDYVDTKFHTRITNRPTRNLDNYLVPDPQVLNYLFTANTENIDLGIIEGVMGLYDGLGTDKDAYSTASIAKQLNIPVILVINARATSTSAAAILKGFIDFDKKVPIKGVIINNVMSENHYKLIAGAIHRYLDLPILGYLPHDSTISLPSRQLGLVPDDELPNVDKKIAKVAEDVKAHVDLQKLLSLATSVSEKVVDPFNIPKTRLRLGIAKDKAFNFYYADNIHLLEKTGIELIPFSPISDNHLPDVDALYFGGGYPEEFASRLAANEFLKKEVYEFSQANKPIYAECGGLMYLGKVLKQGENEFPMVGIFDGMSEMTPRLKRFGYCEAYTQVDCMLGNRGQKIVGHEFHHSMFKQLDQQLKPVLLMKKVRDNQIVDTWSGGYQIRKTFASYLHVHFYQNPKLFIQFLNNLGADVQ

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Length
454 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
50.193 kDa
Sequence
MNIKIPRIVIGGTGSGVGKTTIALALTQILRKKGLKVATFKCGPDYLDPTYHSRASQKICHNLDGWLMGKESVLNTFYQACHNVDIAIIEGMMGLFDGHSPNSEIGSTAEIAKWLASPVLVVLDTRGMARTVSAILKGLKIFDPDLNLAGAFANFTGSPSHIQLLKDASTEVPILGGLCKHSEQTFPERHLGLYSASEENVSEEKFNFWGEEGEKSLEVNSILEIANSAPEISIPVSNINTTLKRCKIGIAMDSAFHFYYEENLMRLRQAGAELVFFSPLSDSRLTDVDGLYFGGGYPEVFAPTLSKNKSLLNYIRDLSYKNIPIYAECGGLMYLSKGIKLVEGEFFPMLGLISATSIMEKKLKALGYVEVTTKKETIFGEVGLRFRGHQFRYSDLELDESNPIELVYNLRKRKSDQVSEEGYSKNSILASYIHAHWASNPNLAEGFVQSCLRK

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Length
454 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
50.165 kDa
Sequence
MNIKIPRIVIGGTGSGVGKTTIALALTQILRKKGLKVATFKCGPDYLDPTYHSRASQKICHNLDGWLMGKESVLNTFYQACHNVDIVIIEGMMGLFDGHSPNSEIGSTAEIAKWLASPVLVVLDTRGMARTVSAILKGLKIFDPDLNLAGAFANFTGSPSHIQLLKDASTEVPILGGLCKHSEQTFPERHLGLYSASEENVSEEKFNFWGEEGEKSLEVNSILEIANSAPEISIPVSNINTTLKRCKIGIAMDSAFHFYYEENLMRLRQAGAELVFFSPLSDSKLTDVDGLYFGGGYPEVFAPTLSKNKSLLNYIQDLSYKNIPIYAECGGLMYLSKGIKLVEGEFFPMLGLISATSIMEKKLKALGYVEVTTKKETIFGEVGLRFRGHQFRYSDLELDESNPIELVYNLRKRKSDQVSEEGYSKNSILASYIHAHWASNPNLAEGFVQSCLRK

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Length
454 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
50.355 kDa
Sequence
MKVPRVIIAGTNSGVGKTTTTLAVISALKNKGLKVKPYKVGPDYIDPQFHSLLAGATSDNLDLWMIPRERIFQLLADASTSFNISVIEGVMGLLDGFGSTDEGSTLDLARITGTPIILVIDGYGLSGSAAAIVKGFKDFSGDLLAGVIVTRVSGERHYDLIKKAIEDNTNVRVLGYIEKNDEVRLESRHLGLVQASELNSFSDYIERLSKVTHINVDGIIEIARASRDLDPKFSPLLSRVGYAKIAVAYDSAFDFYYEENFRVLRNLGAELVFFSPLNNEIPPEDTDGLYIGGGYPEVFAKKLAYAVDARENIAKLIKKGVPTLAECGGYMYLTRTIVGQDGIEYPGVGIVPAKTFLTDKLILGYREIVSKTSNMLLRHGETARGHEFHRSTIQFQDKVDHPFVLKYKDRFEEDGYYSNNVVASYVHIHFLSNIAIPKRFVEECIRYSKKREIS

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)
Length
453 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
50.72 kDa
Sequence
MKRVVLTGTGSGVGKTTIATGIMKALSDEHKIQPFKVGPDYIDPSYHNCATGVSSRNLDSFFMSDGQIRQSFKNGMTSSHADYGIIEGVRGLYEGISPTNDIGSTSSIAKALNSPVILIINSRSLVRSAAAMTLGFKALDSRIDIEGVILNNVKSQKHYLKTKEAVEKLANTRVLGGIERDNSISMEQRHLGLIPAVEQERISGLVEKWGELIRENIDLDALMEIMDNSNPIINEYEPIWSPNKTKHKTRIAVPFDEAFNFYYKENLEALEYNNAKIEYFSPIHDEQLPSVDALYIGGGYPEIFKKELSKNTTMLESIKEFSQDNHPIYAECGGLMYLCKTIDSLPMVDVFPYHSMLTKRVQGLSYTIAHVQRDNPILKKNTTYHGHEFHYSKVEYTGSNSNDFAFSMRRGVGITGKYDGLLKNNTLASYIHTHTACLPDFGYNFTQSAYENK

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Length
452 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
49.762 kDa
Sequence
MNKILIAAASSGAGKTTVTLGIMQALKKRGFAVQPFKVGPDYIDTNYHQAITGVASINLDSFLIDDDEMLASLFQKHGESADISVIEGVMGLFDGLGTDRDNASTSFIAKCTKTPVILVVDGKAISTSAAAIVDGFNRFDPELKIAGVIINRVASENHFSLIKGAIERYTDVPVLGYLPKNAAVALPERHLGLVPQEEMTELEAKWELLSDLITTHVDLDKLLEISKSSENLSTSKAQMKVADFSGLRVAYALDAAFHFYYQDNLDLIRLTGAELIPFSPLEDNEVPEADFIYIGGGFPEIFAKQLNDNRSMRKSILAAHEKGIPIYAECGGLMYLGSSLEMEGKQYEMVGVFNGISKMTTRLRKFGYCIAEPLEETLIGKKGMSIRGHEFHHSVFETTETACMKLSKKRDGEIVKEWRGGYQKGNTFASYLHIHFYQNPAILMQMFGAGKR

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Listeria monocytogenes serotype 4b (strain F2365)
Length
452 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
49.818 kDa
Sequence
MNKILIAAASSGTGKTTITLGIMHALKKRGLRVQPFKVGPDYIDTNYHQAITGVASINLDSFLIDDDAMLATLFQKHGESADISVIEGVMGLFDGLGIDRDNSSTSFIAKCTKTPVILVVDGKAISTSAAAIVDGFNRFDPELTIAGVIINRVASENHFSLIKGAIERYTDVPVLGYLPKNAAVALPERHLGLVPKEEMTELETKWELLGDLIAEHVDLDRLLAISKTGAKLTVHPPEIQVPDFSGVRVAYALDAAFHFYYQDNLDFIRSTGATLIPFSPLEEREVPDADFIYIGGGFPEVFAEQLAKNKSMRESILAAHEQGKPIYAECGGLMYLGSSLEMEAESYEMVGVFDGVSKMTTRLRKFGYCIAEPLEDTLLGKKGTAIRGHEFHHSVFETTEPTRMKLTKKRDGKIVKEWHGGYQKGNTFASYLHIHFYQNLLIITHMFGAIER

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Length
452 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
49.766 kDa
Sequence
MNKILIAAASSGTGKTTVTLGIMHALKKRGLRVQPFKVGPDYIDTNYHQAITGVASINLDSFLIDDDAMLAALFEKHGQSADISVIEGVMGLFDGLGIDRDNSSTSFIAKCTKTPVILVVDGKAISTSAAAIVDGFNRFDPELTIAGVIINRVASENHFSLIKGAIERYTDVPVLGYLPKNAAVALPERHLGLVPKEEMTELETKWEVLGDLIAEHVDLDRLLAISKTGAKLTVHPPEIQVPDFSGMRVAYALDAAFHFYYQDNLDFIRSTGATLIPFSPLEEREVPDADFIYIGGGFPEVFAERLAKNKSMHESILAAHEQGKPIYAECGGLMYLGSSLEMEAESYEMVGVFDGVSKMTTRLRKFGYCIAEPLEDTLLGKKGTAIRGHEFHHSVFETTEPTRMKLTKKRDGETVKEWHGGYQKGNTFASYLHIHFYQNLAMITHMFGAIER

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Streptococcus sanguinis (strain SK36)
Length
452 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
50.185 kDa
Sequence
MKQFMLAGVSSGVGKTTVTLGILKALADRGYQVQPYKIGPDYIDTAYHSRITKRPSRNVDSFMIPDDQSLAWSYYKWHGDADVAVVEGVMGLFDGLGTDKDCASSASVAKKLGIPVVLIIDGKATSTSAAAMVHGFATFDPDLDIAGVIINRVASQTHFELIKGAIERYTDVEVLGYLPKNATAELPSRHLGLIPDVEMDDLDRRFEDLGAATAKHINLDRLLEKAELPDKRMTNPFRISNDQPLTLAYALDDAFHFYYEDNLDFLRELNVQLVPFSPLKDKELPAADAYYFGGGFPEVYAQELMANADFRASVKKAHEQGRPIYAECGGLMYLGELLEVEGQVYEMVGIFKGKSLMTPGLKSFGYCQAETQVDSLFGPKGTAVRGHEFHHSVFETEEDTVLKLEKVRDGQVVAAWTGGYQKGRTFASYLHVHFYQDEQLLANWLDYIKEAN

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)
Length
451 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
50.12 kDa
Sequence
MRIILAGTGSAVGKTTIATGIMKALSEEYNVQPFKVGPDYIDPTYHTLATGNTSRNLDSFFMKEGQVRDAFLKAMEKKDIAIIEGVRGLYEGIDSINDIGSTASIAKSLNAPVILIINSRSLVKSAAALVLGFKALDPEINIAGVILNKVKNNAHYLKTKKSIEEITDVEVIGGIIRDDSISIEQRHLGLVPAVERENSLSFIELWSNIIKESIDLDRLVEIAKEAPKLTSPREDIWNKLNKQKVKIGVAYDEVFNFYYKENIESLEANSCKVEYFSPLKDESLPDVDGLYIGGGYPELFSKELSQNTVLLKQIKQFHMENRPIFAECGGLMYLMNSIHEDKQVGVYPYNSILTDKVQALKYTIAEVKKDNIISKKGEKFNGHEFHYSKVLVDNSNIKHDLAFNILRGKGSYNNQDGFMEKNTLASYVHTHVAAMPNFGGNLAISAREVGG

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Methanococcus maripaludis (strain C5 / ATCC BAA-1333)
Length
447 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
50.199 kDa
Sequence
MKRVVIAGTSSMVGKTTISTGIMKALSKKNNVQPYKIGPDYIDPTYHTEATKNKSRNLDSFFMDEMQVRSIFKRHSKNKDINVIEGVRGLYEGISPYNDVGSTASVSKTLNAPVILLMDARSLTRSAAAIIKGFKSFDTELNIKGVIFNKIRGEGHLNKLKEAVKYYDNDIEIIGAIPRDDGLSVSQRHLGLVPTPENKQKLLERIDLWGNTVEECLDIEKIVELSDESFDFEVDEKNKEETLWKVEKNNSKIAVAFDESFNFYYWDNFDALEENGAKIKFFSPLNDVEVPDCDTIYLGGGYPELFSEKLSNNKSMIDSIRNFDGKIYGECGGLMYLTNSIDGKEMLKLIDADAVMTPNVQGLSYVKGTFEKDCIIGEKSKEFKAHEFHYSKLININENDFSYRINRGKGIINSMDGITSKDGDIVGGYAHQHCIGNPYFAANLSKT

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Methanococcus maripaludis (strain C7 / ATCC BAA-1331)
Length
447 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
50.015 kDa
Sequence
MKRIVIAGTSSMVGKTTISTGIMKALSKKNNVQPYKIGPDYIDPTYHTEATENKSRNLDSFFMDKLQIRSLFKKHSKNKDISVIEGVRGLYEGISPYNDIGSTASVAKTLNAPVILLMDARSLTRSAAAIIKGFKSFDTELNIKGVIFNKIRGEGHLNKLKEAVKYYDNEIEIIGAIPRDEGLSVSQRHLGLVPTPENKQGLLERIDLWGNTVEECLDIEKIVELSDKSFDFCVDEKNKDETLWKVEKNNSKIAVAFDESFNFYYWDNFDAMEENGAKLKFFSPLNDSEVPDCDTIYLGGGYPEIFSEKLSENKSMIDSIRNFDGKIYGECGGLMYLTNSIDGKEMLKLIDANAVMTPNVQGLSYVKGTFEKDCIIGEKSKEFKAHEFHYSKLININENDFSYRINRGKGIINSMDGITSKGGDIVGGYAHQHCIGNPYFAASLSKI

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Length
447 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
48.848 kDa
Sequence
MRVVLAGTGSAVGKTTIATGIMKALSGRGVQPFKVGPDYIDPSYHTMATGNTSRNIDSFFMTEAQIREAFTRAMKLSGSRMGIIEGVRGLYEGISPIGDTGSTASVAKALDAPVVLIINSRSLVKSAAAMVLGFRSLDREVKIEGVILNQVKNRRHYLKTRRAVEELTGTAVIGGIPRSSELEVEQRHLGLVPAVERDTIAAQIEKWGLAMEEYIDLEALQDIMSSAGKIRGERQPLWQRGNRKRVRIGVAIDEAFNFYYQENIEALEDNAASVVPFSPIHDEELPDVDAVYIGGGYPEIFAAELESNTSMRKSIQRFHADGRPIFGECGGLMYLMSSIDEREMCGVFPHPAEMTGRVQGLSYVIAEAVMDNLITEAGDKFRGHEFHYSRVLGASGGKFAFRVLRGRGIVDSLDGITSGSSLASYIHIHAASCPQFAANFTRNAWEF

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)
Length
447 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
49.969 kDa
Sequence
MKRVVIAGTSSMVGKTTISTGIMNALSKKNNVQPYKVGPDYIDPTYHTKATENTSRNLDSFFMDETQIRSLFKRHSQNKDISIIEGVRGLFEGISPYNDVGSTASVAKTIDSPIILLMDARSLTRSAAAIIKGFKSFDSELNIKGVIFNKIRGDGHLNKLKEAVKYYDGEIEIVGAIKRDENLAVAERHLGLVPTPEKTEELGKQIEFWGDTVLECLDIDKIIEISDVDFEIPVDNKNKDETLWKVDKNSSKIAIAFDESFNFYYHDNFDALKENGAKLEFFSPIHDFEIPNCDILYLGGGYPEIFSKELSKNTSMIESIRNFDGKIYGECGGLMYLTNSINGVDMLKLINADSIMTKNVQGLSYVIGSFKKDCIIGKEKETFKAHEFHYSKLININENDFSYEINRGTGIIDKLDGISIKDGRIVGGYAHQHAVGNPYFASCLSKL

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Length
443 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
50.206 kDa
Sequence
MIMKRVVIAGTSSEVGKTVISTGIMKALSKKYNVQGYKVGPDYIDPTYHTIATGNKSRNLDSFFMNKEQIKYLFQKHSKDKDISVIEGVRGLYEGISAIDDIGSTASVAKALDSPIILLVNAKSLTRSAIAIIKGFMSFDNVKIKGVIFNFVRSENHIKKLKDAMSYYLPDIEIIGFIPRNEDFKVEGRHLGLVPTPENLKEIESKIVLWGELVEKYLDLDKIVEIADEDFEEVDDVFLWEVNENYKKIAVAYDKAFNFYYWDNFEALKENKAKIEFFSPLKDSEVPDADILYIGGGYPELFKEELSRNKEMIESIKEFDGYIYGECGGLMYITKSIDNVPMVGLLNCSAVMTKHVQGLSYVKAEFLEDCLIGRKGLKFKGHEFHYSKLVNIKEERFAYKIERGRGIINNLDGIFNGKVLAGYLHNHAVANPYFASSMVNFGE

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Length
443 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
48.537 kDa
Sequence
MKVPRLIVAGTESGAGKTTITISIILKLLANQMKVKPYKIGPDYIDPQFHRLASGVPSENLDLWMMNDDQIRYLLIEGSREFDISVIEGVMGLFDGAGSDFTGSTYDLARRTGTPIVLVIDGYGISATAAAIVSGIKAYAGELLRGVIVTRVSGESHYRLIRDAVEEKTGVPVLGYMIRNEKAVLESRHLGLVQAYEIDEIREIFGAIDSSTVIDMHQIIDIARSADKLETLYSPEIERLGTFKVSVAMDSAFDFYYEENLRMLKRMGASIRYFSPMGNEVPDADSDLIYLGGGYPEVFAGKLQSATDTIEAIRHAASIGTGVYAECGGYMFLCRSLESTDGHIYGGVGIIPASVYMDASLVIGYREISAKRDTSILRAGETARGHEFHKSRIRFDGPYDHPFVLKSRSSSFEDGFSSGSVTATYAHIHFLSNPRVAENLLIA

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
Length
440 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
49.267 kDa
Sequence
MKINSIIIGAPSSSSGKTTISIGIMRALSRRLRVQPFKVGPDYIDPGYHNIATGRFSSNLDTWMSSREKMKEIFIKRSTGSDISIIEGVMGLYDGKQPDKDTGSTAEVARTLKSPVIIVIDISAMARTAAAIILGLIKMDKRLRISGVILNNAGSDYHCSIVRTAIEKYTGIPVIGCVKRSDDLKIDDRYLGLKTAMEDDNSGKIDKIADIIERSVDLDLLIKISKESGDISFKSGLFSKKNVNRVRIAIAYDAAFNFYYYDNIEMLKMYGAEIVYFSPLNDYKLPEADGLYIGGGFPELFAERLSDNYSIKKDIMEFFNSGRPVFAECGGYMYLSRGIKINGKYYEMASIINGESYMDSLILGYRNIRAESNNILMMGGWHVKGHEFHYSRLNVNANAYKTERGPDGISTKNLLAGYMHLYFPSNPRIPERFVRSCYNV

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Length
437 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
49.161 kDa
Sequence
MRFPRIIISSDRSNSGKTIISSALMRVLSRKMKVRGFKAGPDFIDPKYHTLAARVPSINLDLWLMGIEGVKKSLIRYGKGYDIGIIEGVMGLYDGINVNYSTYELSEVTKTPIILVVNCSNVSSTVGAIVKGLKDYRNARIRGVIFNQIGSETHYNYCKSSIKEVQVLGYIKYDRNFSVPSRHLGLFTTEDFKETENVLQSVSKAIEESVDIDKIIEIANSAEELQEVDEAISNDELDTKKGIAAIAYDSAFNFYYSENIDLLRYKYQIEFFSPLLNEKIDNPSLIYVGGGYPELHLNELEKSSSTIRWIKKEAEKGTKILAECGGLMYLSKEIIADKSYKMVNLFDISIKAKDKLTIGYTELDVLSDNILGRKGEVLRGHEFHVSKAINLGNDVKFSMKNRIGKGIWENKDGAIVYNTLASYSHFHFSSARGLLSF

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Length
434 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
49.346 kDa
Sequence
MKRILLSSDRSGSGKTLITSAIMRALSKKYKVRGFKAGPDFIDPGYHKIATGFPSINLDLWMMGKNNVKRSLAKYGKEFDIGIIEGVMGLYDGVDTLYSTYELAKVTKTPIILIINCSNIGSTVGAIVKGLKYYRSDVSIRGVIFNKIASETHYNYCRNAVEDVEVLGYVPFDKNLEIKSRHLGLVTVEDNREVQNLIRYASELVEKYVDLDKIYEMASDEDLEIDLPEDNESNGVKRKMAIAYDPAFSFYYQENLDILKNKYELEFFSPLNNEYVEDAEAIYIGGGYPELHLNELEKSTRTKKWLKNMSYAGVKIYAECGGLMYLSKNLIDENNKNHSMTGIFDIDIKTKDKLTIGYTELEAVKENFIVNKNNVVRGHEFHVSKPISVNEKEFVFKVRIGKGIINKLDGVKSNNTVASYSHLHFSNFQLRIVF

Gene
cbiA
Protein
Cobyrinate a,c-diamide synthase
Organism
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Length
434 amino acids
Function
Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
Similarity
Belongs to the CobB/CbiA family.
Mass
49.056 kDa
Sequence
MRFPRIIISSDRSNSGKTLVTAGLIKVLSKRYKVRGYKVGPDFIDPMYHKIASGHPVINLDLWLMGESGVYSSLAKYGKHFDLGIIEGVMGLYDGLYEDYSTYKLSELTHTPLILVINCSNLSSTVGAIVKGLREYRNANVRGVIFNYIASEKHLDYCKKSIPENVEVLGYLPIDKSLSVPSRHLGLYTTEDFKNAKDVINATANLIEMNVDVDKIVEIAEEANELQESNEIEERNVVGKAYVAYDSAFSFYYDENIDILKKRYDVEFFSPLNNDAPADQPSFIYIGGGYPELHLEELENSTKTKDWIKRNVEKGVKLLAECGGFMFLSNEIINEKSYRMIGLYDIQIKAKDKLTIGYTELETEKDNLLSSKGESIRGHEFHVSKAVSVGDVNFAFKNKHGKGIWNGKDGVYVENSLGSYSHFHFSRTRRLLSF