Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

GDP-L-fucose synthase

Gene

fcl

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Enzyme 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

  • GDP-L-fucose synthase activity Source: EcoCyc
  • isomerase activity Source: UniProtKB-KW
  • NADP+ binding Source: UniProtKB-HAMAP

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciEcoCyc:FCL-MONOMER.
ECOL316407:JW2037-MONOMER.
MetaCyc:FCL-MONOMER.
BRENDAi1.1.1.271. 2026.
UniPathwayiUPA00128; 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

Complete GO annotation...

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

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.
STRINGi511145.b2052.

Structurei

Secondary structure

1321
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Turni10 – 12Combined sources3
Helixi14 – 23Combined sources10
Beta strandi29 – 32Combined sources4
Turni36 – 38Combined sources3
Helixi44 – 54Combined sources11
Beta strandi57 – 61Combined sources5
Helixi69 – 74Combined sources6
Helixi76 – 96Combined sources21
Beta strandi101 – 105Combined sources5
Helixi108 – 110Combined sources3
Beta strandi117 – 119Combined sources3
Helixi121 – 123Combined sources3
Helixi131 – 133Combined sources3
Helixi134 – 154Combined sources21
Beta strandi157 – 163Combined sources7
Beta strandi165 – 168Combined sources4
Helixi180 – 194Combined sources15
Beta strandi197 – 203Combined sources7
Beta strandi211 – 213Combined sources3
Helixi214 – 226Combined sources13
Helixi229 – 234Combined sources6
Beta strandi243 – 246Combined sources4
Helixi253 – 264Combined sources12
Beta strandi268 – 273Combined sources6
Beta strandi281 – 283Combined sources3
Helixi288 – 292Combined sources5
Helixi301 – 314Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BSVX-ray2.20A1-321[»]
1BWSX-ray2.20A1-321[»]
1E6UX-ray1.45A1-321[»]
1E7QX-ray1.60A1-321[»]
1E7RX-ray1.60A1-321[»]
1E7SX-ray1.50A1-321[»]
1FXSX-ray2.30A1-321[»]
1GFSX-ray2.20A1-321[»]
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.
OMAiRMHTAKL.
PhylomeDBiP32055.

Family and domain databases

CDDicd05239. GDP_FS_SDR_e. 1 hit.
Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_00956. GDP_fucose_synth. 1 hit.
InterProiIPR001509. Epimerase_deHydtase.
IPR028614. GDP_fucose/colitose_synth.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]
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.
PATRICi32119437. VBIEscCol129921_2129.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BSVX-ray2.20A1-321[»]
1BWSX-ray2.20A1-321[»]
1E6UX-ray1.45A1-321[»]
1E7QX-ray1.60A1-321[»]
1E7RX-ray1.60A1-321[»]
1E7SX-ray1.50A1-321[»]
1FXSX-ray2.30A1-321[»]
1GFSX-ray2.20A1-321[»]
ProteinModelPortaliP32055.
SMRiP32055.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259691. 221 interactors.
IntActiP32055. 2 interactors.
STRINGi511145.b2052.

Proteomic databases

PaxDbiP32055.
PRIDEiP32055.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75113; AAC75113; b2052.
BAA15908; BAA15908; BAA15908.
GeneIDi946563.
KEGGiecj:JW2037.
eco:b2052.
PATRICi32119437. VBIEscCol129921_2129.

Organism-specific databases

EchoBASEiEB1736.
EcoGeneiEG11788. fcl.

Phylogenomic databases

eggNOGiENOG4105C30. Bacteria.
COG0451. LUCA.
HOGENOMiHOG000168011.
InParanoidiP32055.
KOiK02377.
OMAiRMHTAKL.
PhylomeDBiP32055.

Enzyme and pathway databases

UniPathwayiUPA00128; UER00191.
UPA00980.
BioCyciEcoCyc:FCL-MONOMER.
ECOL316407:JW2037-MONOMER.
MetaCyc:FCL-MONOMER.
BRENDAi1.1.1.271. 2026.

Miscellaneous databases

EvolutionaryTraceiP32055.
PROiP32055.

Family and domain databases

CDDicd05239. GDP_FS_SDR_e. 1 hit.
Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_00956. GDP_fucose_synth. 1 hit.
InterProiIPR001509. Epimerase_deHydtase.
IPR028614. GDP_fucose/colitose_synth.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFCL_ECOLI
AccessioniPrimary (citable) accession number: P32055
Secondary accession number(s): P76382
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.