GDP-L-fucose synthase

Details

Name
GDP-L-fucose synthase
Synonyms
  • 1.1.1.271
  • GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase
  • wcaG
  • yefB
Gene Name
fcl
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011364|GDP-L-fucose synthase
MSKQRVFIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLLDSRAVHDFFASERIDQVY
LAAAKVGGIVANNTYPADFIYQNMMIESNIIHAAHQNDVNKLLFLGSSCIYPKLAKQPMA
ESELLQGTLEPTNEPYAIAKIAGIKLCESYNRQYGRDYRSVMPTNLYGPHDNFHPSNSHV
IPALLRRFHEATAQNAPDVVVWGSGTPMREFLHVDDMAAASIHVMELAHEVWLENTQPML
SHINVGTGVDCTIRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQLGWYHEIS
LEAGLASTYQWFLENQDRFRG
Number of residues
321
Molecular Weight
36140.87
Theoretical pI
6.89
GO Classification
Functions
GDP-L-fucose synthase activity / isomerase activity / NADP+ binding
Processes
'de novo' GDP-L-fucose biosynthetic process / colanic acid biosynthetic process
Components
cytoplasm
General Function
Nadp+ binding
Specific Function
Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0011365|GDP-L-fucose synthase (fcl)
ATGAGTAAACAACGAGTTTTTATTGCTGGTCATCGCGGGATGGTCGGTTCCGCCATCAGG
CGGCAGCTCGAACAGCGCGGTGATGTGGAACTGGTATTACGCACCCGCGACGAGCTGAAC
CTGCTGGACAGCCGCGCCGTGCATGATTTCTTTGCCAGCGAACGTATTGACCAGGTCTAT
CTGGCGGCGGCGAAAGTGGGCGGCATTGTTGCCAACAACACCTATCCGGCGGATTTCATC
TACCAGAACATGATGATTGAGAGCAACATCATTCACGCCGCGCATCAGAACGACGTGAAC
AAACTGCTGTTTCTCGGATCGTCCTGCATCTACCCGAAACTGGCAAAACAGCCGATGGCA
GAAAGCGAGTTGTTGCAGGGCACGCTGGAGCCGACTAACGAGCCTTATGCTATTGCCAAA
ATCGCCGGGATCAAACTGTGCGAATCATACAACCGCCAGTACGGACGCGATTACCGCTCA
GTCATGCCGACCAACCTGTACGGGCCACACGACAACTTCCACCCGAGTAATTCGCATGTG
ATCCCAGCATTGCTGCGTCGCTTCCACGAGGCGACGGCACAGAATGCGCCGGACGTGGTG
GTATGGGGCAGCGGTACACCGATGCGCGAATTTCTGCACGTCGATGATATGGCGGCGGCG
AGCATTCATGTCATGGAGCTGGCGCATGAAGTCTGGCTGGAGAACACCCAGCCGATGTTG
TCGCACATTAACGTCGGCACGGGCGTTGACTGCACTATCCGCGAGCTGGCGCAAACCATC
GCCAAAGTGGTGGGTTACAAAGGCCGGGTGGTTTTTGATGCCAGCAAACCGGATGGCACG
CCGCGCAAACTGCTGGATGTGACGCGCCTGCATCAGCTTGGCTGGTATCACGAAATCTCA
CTGGAAGCGGGGCTTGCCAGCACTTACCAGTGGTTCCTTGAGAATCAAGACCGCTTTCGG
GGGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP32055
UniProtKB Entry NameFCL_ECOLI
GenBank Protein ID1407613
GenBank Gene IDU38473
General References
  1. Aoyama K, Haase AM, Reeves PR: Evidence for effect of random genetic drift on G+C content after lateral transfer of fucose pathway genes to Escherichia coli K-12. Mol Biol Evol. 1994 Nov;11(6):829-38. [Article]
  2. Stevenson G, Andrianopoulos K, Hobbs M, Reeves PR: Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid. J Bacteriol. 1996 Aug;178(16):4885-93. [Article]
  3. Itoh T, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Kasai H, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Seki Y, Horiuchi T, et al.: A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):379-92. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Andrianopoulos K, Wang L, Reeves PR: Identification of the fucose synthetase gene in the colanic acid gene cluster of Escherichia coli K-12. J Bacteriol. 1998 Feb;180(4):998-1001. [Article]
  7. Menon S, Stahl M, Kumar R, Xu GY, Sullivan F: Stereochemical course and steady state mechanism of the reaction catalyzed by the GDP-fucose synthetase from Escherichia coli. J Biol Chem. 1999 Sep 17;274(38):26743-50. [Article]
  8. Rizzi M, Tonetti M, Vigevani P, Sturla L, Bisso A, Flora AD, Bordo D, Bolognesi M: GDP-4-keto-6-deoxy-D-mannose epimerase/reductase from Escherichia coli, a key enzyme in the biosynthesis of GDP-L-fucose, displays the structural characteristics of the RED protein homology superfamily. Structure. 1998 Nov 15;6(11):1453-65. [Article]
  9. Somers WS, Stahl ML, Sullivan FX: GDP-fucose synthetase from Escherichia coli: structure of a unique member of the short-chain dehydrogenase/reductase family that catalyzes two distinct reactions at the same active site. Structure. 1998 Dec 15;6(12):1601-12. [Article]
  10. Rosano C, Bisso A, Izzo G, Tonetti M, Sturla L, De Flora A, Bolognesi M: Probing the catalytic mechanism of GDP-4-keto-6-deoxy-d-mannose Epimerase/Reductase by kinetic and crystallographic characterization of site-specific mutants. J Mol Biol. 2000 Oct 13;303(1):77-91. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02897AcetylphosphateexperimentalunknownDetails
DB03461Nicotinamide adenine dinucleotide phosphateexperimentalunknownDetails