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Fuca

Gene
Fuca
Protein
Putative alpha-L-fucosidase
Organism
Drosophila melanogaster
Length
494 amino acids
Function
Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Similarity
Belongs to the glycosyl hydrolase 29 family.
Mass
57.723 kDa
Sequence
MAISAWMPLLVALIVVWISAAEVDAQVPGPRTRYQPNWASLDQRPLPQWYDDAKVGIFLHYGVYSVPSFGSEWFWTNWKNLRNPEYVQFMQRNYKPDFTYQEFASQFTAELFNATKWALLFKDSGARYVVLTSKHHDGFTLWPSKNSYGWNSMDVGPKRDIVKELAAAIRKESDLRFGLYYSLFEWFNPLWTDDKLHLLMQQHFVERKVRPEQMELVQQYLPEIIWSDGDWEAPAKYWRSEEFIAWLYNDSPVRDTVVTNDRWGFGTACMHGDFYNCADRFNPGVLQAHKWENAFTLDRTSWGQRFDVSLSDFMTSKEVIKEIITTVSCNGNVLINVGPTKFGTILPIFEERLRDMGRWLKFNGEGIYGSVPWIYQNDTINGNVWYTRQKEASNGKITIYAFVLEYPYDTNELDIYPLGKDINIFRNVMLTGIDMGTGGDILNEQSTEVVMLGMEDTKIKWNADHNRLHIVFPPKNHIDKRGLDYAWTFKITIT

Gene
Fuca
Protein
Putative alpha-L-fucosidase
Organism
Drosophila melanogaster
Length
494 amino acids
Function
Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins.
Similarity
Belongs to the glycosyl hydrolase 29 family.
Mass
57.723 kDa
Sequence
MAISAWMPLLVALIVVWISAAEVDAQVPGPRTRYQPNWASLDQRPLPQWYDDAKVGIFLHYGVYSVPSFGSEWFWTNWKNLRNPEYVQFMQRNYKPDFTYQEFASQFTAELFNATKWALLFKDSGARYVVLTSKHHDGFTLWPSKNSYGWNSMDVGPKRDIVKELAAAIRKESDLRFGLYYSLFEWFNPLWTDDKLHLLMQQHFVERKVRPEQMELVQQYLPEIIWSDGDWEAPAKYWRSEEFIAWLYNDSPVRDTVVTNDRWGFGTACMHGDFYNCADRFNPGVLQAHKWENAFTLDRTSWGQRFDVSLSDFMTSKEVIKEIITTVSCNGNVLINVGPTKFGTILPIFEERLRDMGRWLKFNGEGIYGSVPWIYQNDTINGNVWYTRQKEASNGKITIYAFVLEYPYDTNELDIYPLGKDINIFRNVMLTGIDMGTGGDILNEQSTEVVMLGMEDTKIKWNADHNRLHIVFPPKNHIDKRGLDYAWTFKITIT

Gene
fucA
Protein
L-fuculose phosphate aldolase
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
216 amino acids
Function
Involved in the degradation of L-fucose and D-arabinose. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
Similarity
Belongs to the aldolase class II family. AraD/FucA subfamily.
Mass
23.944 kDa
Sequence
MNRAELSQKIIDTCLEMTKLGLNQGTAGNVSVRYKDGMLITPTGMPYHLMKTENIVYVDGNGKHEENKLPSSEWQFHLSVYHTRPEANAVVHNHSIHCAGLSILEKPIPAIHYMVAVSGTDHIPCVPYATFGSHKLASYVATGIKESKAILLAHHGLITCGENLDKALWLAQEVEVLASWYLKLLSTGLEIPLLSKEQMQVVLGKFHTYGLRIEES

Gene
fucA
Protein
L-fuculose phosphate aldolase
Organism
Escherichia coli O157:H7
Length
215 amino acids
Function
Involved in the degradation of L-fucose and D-arabinose. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
Similarity
Belongs to the aldolase class II family. AraD/FucA subfamily.
Mass
23.785 kDa
Sequence
MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFIDGNGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQLYLTTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE

Gene
fucA
Protein
L-fuculose phosphate aldolase
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
215 amino acids
Function
Involved in the degradation of L-fucose and D-arabinose. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
Similarity
Belongs to the aldolase class II family. AraD/FucA subfamily.
Mass
23.757 kDa
Sequence
MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFIDGNGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTAVSILNRPIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACEANLEKALWLAHEVEVLAQLYLTTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE

Gene
fucA
Protein
L-fuculose phosphate aldolase
Organism
Escherichia coli (strain K12)
Length
215 amino acids
Function
Involved in the degradation of L-fucose and D-arabinose (PubMed:13898172). Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde (PubMed:13898172, Ref.8, Ref.9, PubMed:10821675, PubMed:11054289). Also able to catalyze the reversible cleavage of D-ribulose 1-phosphate, but FucA has a higher affinity for L-fuculose 1-phosphate and L-lactaldehyde than for D-ribulose 1-phosphate and glycolaldehyde, respectively (PubMed:4928018). FucA possesses a high specificity for the dihydroxyacetone phosphate (DHAP), but accepts a great variety of different aldehydes and has a strong preference for L-configurated alpha-hydroxy aldehydes (PubMed:13898172, Ref.8, PubMed:10821675). FucA generates a vicinal diol unit having the absolute (3R,4R)-cis configuration (D-erythro) (Ref.8, PubMed:10821675).
Similarity
Belongs to the aldolase class II family. AraD/FucA subfamily.
Mass
23.775 kDa
Sequence
MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFIDGNGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTAVSILNRSIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQLYLTTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE

Gene
fucA
Protein
L-fuculose phosphate aldolase
Organism
Shigella flexneri
Length
215 amino acids
Function
Involved in the degradation of L-fucose and D-arabinose. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
Similarity
Belongs to the aldolase class II family. AraD/FucA subfamily.
Mass
23.775 kDa
Sequence
MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFIDGNGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTAVSILNRSIPAIHYMIAAAGGNSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQLYLTTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE

Gene
fucA
Protein
L-fuculose phosphate aldolase
Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Length
181 amino acids
Function
Involved in the biosynthesis of the coenzyme F420 which requires phospholactate produced via the aldol cleavage of L-fuculose 1-phosphate and the NAD(+)-dependent oxidation of (S)-lactaldehyde (PubMed:16585745). Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and S-lactaldehyde (Ref.2, PubMed:16585745, PubMed:17927915, PubMed:22418259). FucA possesses a high specificity for the dihydroxyacetone phosphate (DHAP), but accepts a great variety of different aldehydes such as DL-glyceraldehyde and glycolaldehyde (PubMed:16585745, PubMed:17927915).
Similarity
Belongs to the aldolase class II family. AraD/FucA subfamily.
Mass
20.47 kDa
Sequence
MDKKQFIKICRKLYDRKYVVGSGGNVSVKEGDKIYLTPTGSILGFLKEDDIAEMDLDGNVIKGKPTSEKNLHLMIYRKRNDINAIIHTHSLISTFLSTINKEIELLTPEGKIFLKKIGYVDYYEAGSLKLAEETAKRDEDVIILKNHGVVCLGKDLIDAYIKVEVLEEQAKLTLLNLLVKK

Gene
fucA
Protein
L-fuculose phosphate aldolase
Organism
Methanococcus maripaludis (strain C5 / ATCC BAA-1333)
Length
181 amino acids
Function
Involved in the biosynthesis of the coenzyme F420 which requires phospholactate produced via the aldol cleavage of L-fuculose 1-phosphate and the NAD(+)-dependent oxidation of (S)-lactaldehyde. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and S-lactaldehyde.
Similarity
Belongs to the aldolase class II family. AraD/FucA subfamily.
Mass
20.191 kDa
Sequence
MNLSNFIKICHLLYDRKYVVGSGGNVSIKNKNLIYITPTGSILGFLNEEDICVADIEGNILKGKPTSELNMHLKIYQNKESINAIVHTHSMYCTAFSALDKKLELLTPEAEIFIKKIAYVDYFPCGSLELAENVSACVEDSIILKNHGIVTLGKDITEAYVKTEVLEEIAQLNYIMNNLGE

Gene
fucA
Protein
L-fuculose phosphate aldolase
Organism
Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)
Length
181 amino acids
Function
Involved in the biosynthesis of the coenzyme F420 which requires phospholactate produced via the aldol cleavage of L-fuculose 1-phosphate and the NAD(+)-dependent oxidation of (S)-lactaldehyde. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and S-lactaldehyde.
Similarity
Belongs to the aldolase class II family. AraD/FucA subfamily.
Mass
20.301 kDa
Sequence
MDLKEFIKICHLLYDRKYVVGSGGNVSLKKDNLVYITPTGSILGFLNEEDICVVDIAGKIIKGKPTSELNMHLEIYRNKPHVNAVVHTHSMYCTAFSVLDKKLELYTPEAEIFLKKIGYVDYCPCGTLELAECVSSCNEDVLILKKHGIVTLGSTLTEAYIKTEVLEEIAKLNHIVMSFDK

Gene
fucA
Protein
L-fuculose phosphate aldolase
Organism
Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)
Length
180 amino acids
Function
Involved in the biosynthesis of the coenzyme F420 which requires phospholactate produced via the aldol cleavage of L-fuculose 1-phosphate and the NAD(+)-dependent oxidation of (S)-lactaldehyde. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and S-lactaldehyde.
Similarity
Belongs to the aldolase class II family. AraD/FucA subfamily.
Mass
20.464 kDa
Sequence
MDNLKEFIKICHYLYDRKYVVGSGGNVSIKKDNLIYVTPTDSLLGFINEEDIAVVDMDGNIIKGAPTSELYMHLNIYKKRNGVNAIVHTHSLYSTALPMADKEIKLLTPESRIFLKKIGYVDYFEARSMELANEVSKKDEDVIVLKNHGIVCVGKNLMDAYLKTEVMEEISQLNYIIHSL

Gene
fucA
Protein
L-fuculose phosphate aldolase
Organism
Methanococcus maripaludis (strain C7 / ATCC BAA-1331)
Length
180 amino acids
Function
Involved in the biosynthesis of the coenzyme F420 which requires phospholactate produced via the aldol cleavage of L-fuculose 1-phosphate and the NAD(+)-dependent oxidation of (S)-lactaldehyde. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and S-lactaldehyde.
Similarity
Belongs to the aldolase class II family. AraD/FucA subfamily.
Mass
20.039 kDa
Sequence
MDLINFIKICHLLYDRKYVVGSGGNVSIRDGNHIYITPTGSILGFLNEEDVCIVDLNGNIIKGKPTSELNMHLKIYQNKDCVNAIVHTHSMYCTAFSALDKKLELFTPEAEIVVKKIAYVDYSPCGSLELAENVSSCVEDSIILKNHGIVTVGKDITEAYVKTEVLEEIAQLNYIINNLK

Gene
fucA
Protein
L-fuculose phosphate aldolase
Organism
Methanococcus maripaludis (strain S2 / LL)
Length
180 amino acids
Function
Involved in the biosynthesis of the coenzyme F420 which requires phospholactate produced via the aldol cleavage of L-fuculose 1-phosphate and the NAD(+)-dependent oxidation of (S)-lactaldehyde. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and S-lactaldehyde.
Similarity
Belongs to the aldolase class II family. AraD/FucA subfamily.
Mass
20.11 kDa
Sequence
MDLTEFIKICRLLYDRKYVVGSGGNVSIRDGNLIYITPTGLSLGFLTKEDICIADLNGNIIKGKPTSELNMHLKIYQNKDSINAVVHTHSMYCTAFSALDKKLKLVTPEAEMVVKKIAYVDYFPCGSLELAENVSECIEDSIILKNHGIVTLGKDITEAYIKTEVLEEVAQLNYIMNNLK