Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P32055

- FCL_ECOLI

UniProt

P32055 - FCL_ECOLI

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell

    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.
    KOiK02377.
    OMAiIHVMELD.
    OrthoDBiEOG6JB132.
    PhylomeDBiP32055.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    HAMAPiMF_00956. GDP_fucose_synth.
    InterProiIPR001509. Epimerase_deHydtase.
    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

    MSKQRVFIAG HRGMVGSAIR RQLEQRGDVE LVLRTRDELN LLDSRAVHDF    50
    FASERIDQVY LAAAKVGGIV ANNTYPADFI YQNMMIESNI IHAAHQNDVN 100
    KLLFLGSSCI YPKLAKQPMA ESELLQGTLE PTNEPYAIAK IAGIKLCESY 150
    NRQYGRDYRS VMPTNLYGPH DNFHPSNSHV IPALLRRFHE ATAQNAPDVV 200
    VWGSGTPMRE FLHVDDMAAA SIHVMELAHE VWLENTQPML SHINVGTGVD 250
    CTIRELAQTI AKVVGYKGRV VFDASKPDGT PRKLLDVTRL HQLGWYHEIS 300
    LEAGLASTYQ WFLENQDRFR G 321
    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.
    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.
    IPR028614. GDP_fucose_synth.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF01370. Epimerase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 1, 2014
    This is version 127 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