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P32055

- FCL_ECOLI

UniProt

P32055 - FCL_ECOLI

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Protein

GDP-L-fucose synthase

Gene

fcl

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.3 PublicationsUniRule annotation

Catalytic activityi

GDP-beta-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-alpha-D-mannose + NADPH.3 PublicationsUniRule annotation

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

Vmax=363.5 µmol/min/mg enzyme2 Publications

pH dependencei

Optimum pH is 6-6.5.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei107 – 1071Important for catalytic activity
Sitei109 – 1091Important for catalytic activity
Active sitei136 – 1361Proton donor/acceptor1 PublicationUniRule annotation
Binding sitei140 – 1401NADP3 PublicationsUniRule annotation
Sitei140 – 1401Lowers pKa of active site Tyr
Binding sitei179 – 1791NADP3 PublicationsUniRule annotation
Binding sitei187 – 1871SubstrateCurated
Binding sitei202 – 2021SubstrateUniRule annotation
Binding sitei209 – 2091SubstrateUniRule annotation
Binding sitei278 – 2781SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 167NADP3 PublicationsUniRule annotation
Nucleotide bindingi36 – 416NADP3 PublicationsUniRule annotation
Nucleotide bindingi105 – 1084NADP3 PublicationsUniRule annotation
Nucleotide bindingi163 – 1664NADP3 PublicationsUniRule annotation

GO - Molecular functioni

  1. GDP-L-fucose synthase activity Source: EcoCyc
  2. isomerase activity Source: UniProtKB-KW
  3. NADP+ binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' GDP-L-fucose biosynthetic process Source: UniProtKB-HAMAP
  2. colanic acid biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-L-fucose synthaseUniRule annotation (EC:1.1.1.271UniRule annotation)
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11788. fcl.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071S → A: Nearly abolishes catalytic activity. Minor effect of affinity for NADPH and substrate. 1 Publication
Mutagenesisi109 – 1091C → A: Nearly abolishes catalytic activity.
Mutagenesisi136 – 1361Y → E: Abolishes enzyme activity. 1 Publication
Mutagenesisi140 – 1401K → R: Reduces catalytic activity 20-fold. 1 Publication
Mutagenesisi140 – 1401K → S: Nearly abolishes catalytic activity. 1 Publication
Mutagenesisi179 – 1791H → N: Nearly abolishes catalytic activity. 1 Publication
Mutagenesisi187 – 1871R → A: Decreases affinity for the substrate GDP-4-keto-6-deoxymannose. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321GDP-L-fucose synthasePRO_0000174358Add
BLAST

Proteomic databases

PaxDbiP32055.

Expressioni

Gene expression databases

GenevestigatoriP32055.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

IntActiP32055. 2 interactions.
STRINGi511145.b2052.

Structurei

Secondary structure

1
321
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96
Turni10 – 123
Helixi14 – 2310
Beta strandi29 – 324
Turni36 – 383
Helixi44 – 5411
Beta strandi57 – 615
Helixi69 – 746
Helixi76 – 9621
Beta strandi101 – 1055
Helixi108 – 1103
Beta strandi117 – 1193
Helixi121 – 1233
Helixi131 – 1333
Helixi134 – 15421
Beta strandi157 – 1637
Beta strandi165 – 1684
Helixi180 – 19415
Beta strandi197 – 2037
Beta strandi211 – 2133
Helixi214 – 22613
Helixi229 – 2346
Beta strandi243 – 2464
Helixi253 – 26412
Beta strandi268 – 2736
Beta strandi281 – 2833
Helixi288 – 2925
Helixi301 – 31414

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 3-319.
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

eggNOGiCOG0451.
HOGENOMiHOG000168011.
InParanoidiP32055.
KOiK02377.
OMAiIHVMELD.
OrthoDBiEOG6JB132.
PhylomeDBiP32055.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
HAMAPiMF_00956. GDP_fucose_synth.
InterProiIPR001509. Epimerase_deHydtase_N.
IPR028614. GDP_fucose_synth.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti255 – 2562EL → DV no nucleotide entry (PubMed:7815923)Curated
Sequence conflicti255 – 2562EL → DV in AAC77843. (PubMed:8759852)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_490294.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75113; AAC75113; b2052.
BAA15908; BAA15908; BAA15908.
GeneIDi12930697.
946563.
KEGGiecj:Y75_p2015.
eco:b2052.
PATRICi32119437. VBIEscCol129921_2129.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U38473 Genomic DNA. Translation: AAC77843.1 .
U00096 Genomic DNA. Translation: AAC75113.1 .
AP009048 Genomic DNA. Translation: BAA15908.1 .
PIRi C64971.
RefSeqi NP_416556.1. NC_000913.3.
YP_490294.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BSV X-ray 2.20 A 1-321 [» ]
1BWS X-ray 2.20 A 1-321 [» ]
1E6U X-ray 1.45 A 1-321 [» ]
1E7Q X-ray 1.60 A 1-321 [» ]
1E7R X-ray 1.60 A 1-321 [» ]
1E7S X-ray 1.50 A 1-321 [» ]
1FXS X-ray 2.30 A 1-321 [» ]
1GFS X-ray 2.20 A 1-321 [» ]
ProteinModelPortali P32055.
SMRi P32055. Positions 3-319.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P32055. 2 interactions.
STRINGi 511145.b2052.

Proteomic databases

PaxDbi P32055.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75113 ; AAC75113 ; b2052 .
BAA15908 ; BAA15908 ; BAA15908 .
GeneIDi 12930697.
946563.
KEGGi ecj:Y75_p2015.
eco:b2052.
PATRICi 32119437. VBIEscCol129921_2129.

Organism-specific databases

EchoBASEi EB1736.
EcoGenei EG11788. fcl.

Phylogenomic databases

eggNOGi COG0451.
HOGENOMi HOG000168011.
InParanoidi P32055.
KOi K02377.
OMAi IHVMELD.
OrthoDBi EOG6JB132.
PhylomeDBi P32055.

Enzyme and pathway databases

UniPathwayi UPA00128 ; UER00191 .
UPA00980 .
BioCyci EcoCyc:FCL-MONOMER.
ECOL316407:JW2037-MONOMER.
MetaCyc:FCL-MONOMER.

Miscellaneous databases

EvolutionaryTracei P32055.
PROi P32055.

Gene expression databases

Genevestigatori P32055.

Family and domain databases

Gene3Di 3.40.50.720. 2 hits.
HAMAPi MF_00956. GDP_fucose_synth.
InterProi IPR001509. Epimerase_deHydtase_N.
IPR028614. GDP_fucose_synth.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01370. Epimerase. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Evidence for effect of random genetic drift on G+C content after lateral transfer of fucose pathway genes to Escherichia coli K-12."
    Aoyama K., Haase A.M., Reeves P.R.
    Mol. Biol. Evol. 11:829-838(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid."
    Stevenson G., Andrianopoulos K., Hobbs M., Reeves P.R.
    J. Bacteriol. 178:4885-4893(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Identification of the fucose synthetase gene in the colanic acid gene cluster of Escherichia coli K-12."
    Andrianopoulos K., Wang L., Reeves P.R.
    J. Bacteriol. 180:998-1001(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
  7. "Stereochemical course and steady state mechanism of the reaction catalyzed by the GDP-fucose synthetase from Escherichia coli."
    Menon S., Stahl M., Kumar R., Xu G.Y., Sullivan F.
    J. Biol. Chem. 274:26743-26750(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  8. "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."
    Rizzi M., Tonetti M., Vigevani P., Sturla L., Bisso A., Flora A.D., Bordo D., Bolognesi M.
    Structure 6:1453-1465(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.
  9. "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."
    Somers W.S., Stahl M.L., Sullivan F.X.
    Structure 6:1601-1612(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NADP.
    Strain: K12.
  10. "Probing the catalytic mechanism of GDP-4-keto-6-deoxy-d-mannose Epimerase/Reductase by kinetic and crystallographic characterization of site-specific mutants."
    Rosano C., Bisso A., Izzo G., Tonetti M., Sturla L., De Flora A., Bolognesi M.
    J. Mol. Biol. 303:77-91(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH NADP, CATALYTIC ACTIVITY, FUNCTION, PREDICTED SUBSTRATE-BINDING SITES, MUTAGENESIS OF SER-107; TYR-136; LYS-140; HIS-179 AND ARG-187, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE.

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: October 29, 2014
This is version 128 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

External Data

Dasty 3