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Protein

GDP-L-fucose synthase

Gene

fcl

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.UniRule annotation3 Publications

Catalytic activityi

GDP-beta-L-fucose + NADP+ = GDP-4-dehydro-alpha-D-rhamnose + NADPH.UniRule annotation3 Publications

Activity regulationi

Subject to product inhibition by NADP and GDP-fucose.1 Publication

Kineticsi

  1. KM=9 µM for NADPH2 Publications
  2. KM=109 µM for NADH2 Publications
  3. KM=29 µM for GDP-4-keto-6-deoxymannose2 Publications
  1. Vmax=363.5 µmol/min/mg enzyme2 Publications

pH dependencei

Optimum pH is 6-6.5.2 Publications

Pathwayi: GDP-L-fucose biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes GDP-L-fucose from GDP-alpha-D-mannose.UniRule annotation1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. GDP-mannose 4,6-dehydratase (gmd)
  2. GDP-L-fucose synthase (fcl)
This subpathway is part of the pathway GDP-L-fucose biosynthesis via de novo pathway, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes GDP-L-fucose from GDP-alpha-D-mannose, the pathway GDP-L-fucose biosynthesis via de novo pathway and in Nucleotide-sugar biosynthesis.

Pathwayi: colanic acid biosynthesis

This protein is involved in the pathway colanic acid biosynthesis, which is part of Exopolysaccharide biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway colanic acid biosynthesis and in Exopolysaccharide biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei107Important for catalytic activity1
Sitei109Important for catalytic activity1
Active sitei136Proton donor/acceptorUniRule annotation1 Publication1
Binding sitei140NADPUniRule annotation3 Publications1
Sitei140Lowers pKa of active site Tyr1
Binding sitei179NADPUniRule annotation3 Publications1
Binding sitei187SubstrateCurated1
Binding sitei202SubstrateUniRule annotation1
Binding sitei209SubstrateUniRule annotation1
Binding sitei278SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 16NADPUniRule annotation3 Publications7
Nucleotide bindingi36 – 41NADPUniRule annotation3 Publications6
Nucleotide bindingi105 – 108NADPUniRule annotation3 Publications4
Nucleotide bindingi163 – 166NADPUniRule annotation3 Publications4

GO - Molecular functioni

  • coenzyme binding Source: InterPro
  • GDP-L-fucose synthase activity Source: EcoCyc
  • isomerase activity Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Multifunctional enzyme, Oxidoreductase
LigandNADP

Enzyme and pathway databases

BioCyciEcoCyc:FCL-MONOMER
MetaCyc:FCL-MONOMER
BRENDAi1.1.1.271 2026
SABIO-RKiP32055
UniPathwayi
UPA00128;UER00191

UPA00980

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-L-fucose synthaseUniRule annotation (EC:1.1.1.271UniRule annotation3 Publications)
Alternative name(s):
GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductaseUniRule annotation
Gene namesi
Name:fclUniRule annotation
Synonyms:wcaG, yefB
Ordered Locus Names:b2052, JW2037
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11788 fcl

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi107S → A: Nearly abolishes catalytic activity. Minor effect of affinity for NADPH and substrate. 1 Publication1
Mutagenesisi109C → A: Nearly abolishes catalytic activity. 1
Mutagenesisi136Y → E: Abolishes enzyme activity. 1 Publication1
Mutagenesisi140K → R: Reduces catalytic activity 20-fold. 1 Publication1
Mutagenesisi140K → S: Nearly abolishes catalytic activity. 1 Publication1
Mutagenesisi179H → N: Nearly abolishes catalytic activity. 1 Publication1
Mutagenesisi187R → A: Decreases affinity for the substrate GDP-4-keto-6-deoxymannose. 1 Publication1

Chemistry databases

DrugBankiDB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
DB02897 Acetylphosphate

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001743581 – 321GDP-L-fucose synthaseAdd BLAST321

Proteomic databases

PaxDbiP32055
PRIDEiP32055

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

BioGridi4259691, 221 interactors
IntActiP32055, 2 interactors
STRINGi316385.ECDH10B_2202

Structurei

Secondary structure

1321
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP32055
SMRiP32055
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32055

Family & Domainsi

Sequence similaritiesi

Belongs to the NAD(P)-dependent epimerase/dehydratase family. Fucose synthase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C30 Bacteria
COG0451 LUCA
HOGENOMiHOG000168011
InParanoidiP32055
KOiK02377
OMAiIHCAGRV
PhylomeDBiP32055

Family and domain databases

CDDicd05239 GDP_FS_SDR_e, 1 hit
HAMAPiMF_00956 GDP_fucose_synth, 1 hit
InterProiView protein in InterPro
IPR001509 Epimerase_deHydtase
IPR028614 GDP_fucose/colitose_synth
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF01370 Epimerase, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit

Sequencei

Sequence statusi: Complete.

P32055-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKQRVFIAG HRGMVGSAIR RQLEQRGDVE LVLRTRDELN LLDSRAVHDF
60 70 80 90 100
FASERIDQVY LAAAKVGGIV ANNTYPADFI YQNMMIESNI IHAAHQNDVN
110 120 130 140 150
KLLFLGSSCI YPKLAKQPMA ESELLQGTLE PTNEPYAIAK IAGIKLCESY
160 170 180 190 200
NRQYGRDYRS VMPTNLYGPH DNFHPSNSHV IPALLRRFHE ATAQNAPDVV
210 220 230 240 250
VWGSGTPMRE FLHVDDMAAA SIHVMELAHE VWLENTQPML SHINVGTGVD
260 270 280 290 300
CTIRELAQTI AKVVGYKGRV VFDASKPDGT PRKLLDVTRL HQLGWYHEIS
310 320
LEAGLASTYQ WFLENQDRFR G
Length:321
Mass (Da):36,141
Last modified:November 1, 1997 - v2
Checksum:i97077193D79684C7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti255 – 256EL → DV no nucleotide entry (PubMed:7815923).Curated2
Sequence conflicti255 – 256EL → DV in AAC77843 (PubMed:8759852).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38473 Genomic DNA Translation: AAC77843.1
U00096 Genomic DNA Translation: AAC75113.1
AP009048 Genomic DNA Translation: BAA15908.1
PIRiC64971
RefSeqiNP_416556.1, NC_000913.3
WP_000043654.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC75113; AAC75113; b2052
BAA15908; BAA15908; BAA15908
GeneIDi946563
KEGGiecj:JW2037
eco:b2052
PATRICifig|1411691.4.peg.199

Similar proteinsi

Entry informationi

Entry nameiFCL_ECOLI
AccessioniPrimary (citable) accession number: P32055
Secondary accession number(s): P76382
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 1, 1997
Last modified: September 12, 2018
This is version 153 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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