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Protein

L-fucose isomerase

Gene

fucI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts the aldose L-fucose into the corresponding ketose L-fuculose. Is also able to convert D-arabinose into D-ribulose, but this isomerase has a higher affinity for fucose and fuculose than for arabinose and ribulose, respectively.

Catalytic activityi

L-fucopyranose = L-fuculose.1 Publication
D-arabinose = D-ribulose.1 Publication

Cofactori

Kineticsi

  1. KM=17 mM for L-fucose
  2. KM=35 mM for D-arabinose
  3. KM=1.4 mM for L-fuculose
  4. KM=11 mM for D-ribulose

    Pathway:iL-fucose degradation

    This protein is involved in step 1 of the subpathway that synthesizes L-lactaldehyde and glycerone phosphate from L-fucose.
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. L-fucose isomerase (fucI)
    2. L-fuculokinase (fucK)
    3. L-fuculose phosphate aldolase (fucA)
    This subpathway is part of the pathway L-fucose degradation, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-lactaldehyde and glycerone phosphate from L-fucose, the pathway L-fucose degradation and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei337 – 3371Proton acceptor1 Publication
    Metal bindingi337 – 3371Manganese
    Active sitei361 – 3611Proton acceptor1 Publication
    Metal bindingi361 – 3611Manganese
    Metal bindingi528 – 5281Manganese

    GO - Molecular functioni

    • arabinose isomerase activity Source: EcoCyc
    • identical protein binding Source: IntAct
    • L-fucose isomerase activity Source: EcoCyc
    • manganese ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    • D-arabinose catabolic process Source: EcoCyc
    • L-fucose catabolic process Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism, Fucose metabolism

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:FUCISOM-MONOMER.
    ECOL316407:JW2773-MONOMER.
    MetaCyc:FUCISOM-MONOMER.
    UniPathwayiUPA00563; UER00624.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-fucose isomerase (EC:5.3.1.25)
    Short name:
    FucIase
    Alternative name(s):
    6-deoxy-L-galactose isomerase
    D-arabinose isomerase (EC:5.3.1.3)
    Gene namesi
    Name:fucI
    Ordered Locus Names:b2802, JW2773
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10349. fucI.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 591591L-fucose isomerasePRO_0000204145Add
    BLAST

    Proteomic databases

    PaxDbiP69922.
    PRIDEiP69922.

    Expressioni

    Inductioni

    By L-fucose.

    Interactioni

    Subunit structurei

    Homohexamer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-908978,EBI-908978

    Protein-protein interaction databases

    IntActiP69922. 2 interactions.
    STRINGi511145.b2802.

    Structurei

    Secondary structure

    1
    591
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 147Combined sources
    Turni19 – 213Combined sources
    Helixi22 – 4423Combined sources
    Beta strandi55 – 573Combined sources
    Helixi65 – 7612Combined sources
    Turni77 – 793Combined sources
    Beta strandi80 – 8910Combined sources
    Helixi93 – 964Combined sources
    Beta strandi101 – 1033Combined sources
    Beta strandi105 – 1095Combined sources
    Beta strandi113 – 1153Combined sources
    Helixi117 – 13014Combined sources
    Beta strandi136 – 1383Combined sources
    Helixi153 – 17220Combined sources
    Beta strandi176 – 1827Combined sources
    Helixi188 – 1903Combined sources
    Helixi194 – 2018Combined sources
    Beta strandi204 – 2085Combined sources
    Helixi211 – 2188Combined sources
    Helixi224 – 23714Combined sources
    Helixi247 – 2493Combined sources
    Helixi253 – 27523Combined sources
    Helixi279 – 2824Combined sources
    Helixi286 – 2894Combined sources
    Beta strandi294 – 2996Combined sources
    Turni302 – 3087Combined sources
    Helixi313 – 3208Combined sources
    Beta strandi321 – 3244Combined sources
    Beta strandi334 – 3363Combined sources
    Helixi340 – 35314Combined sources
    Beta strandi358 – 3669Combined sources
    Helixi368 – 3758Combined sources
    Helixi381 – 3855Combined sources
    Beta strandi387 – 3904Combined sources
    Helixi398 – 4014Combined sources
    Helixi416 – 4183Combined sources
    Helixi421 – 4299Combined sources
    Beta strandi432 – 4354Combined sources
    Turni438 – 4403Combined sources
    Beta strandi446 – 4494Combined sources
    Beta strandi457 – 46610Combined sources
    Turni467 – 4693Combined sources
    Beta strandi470 – 48011Combined sources
    Helixi485 – 49410Combined sources
    Beta strandi501 – 5066Combined sources
    Helixi512 – 5143Combined sources
    Helixi517 – 5226Combined sources
    Beta strandi525 – 53410Combined sources
    Helixi537 – 54711Combined sources
    Beta strandi551 – 5533Combined sources
    Helixi558 – 5603Combined sources
    Helixi566 – 5694Combined sources
    Helixi574 – 58512Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FUIX-ray2.50A/B/C/D/E/F1-591[»]
    ProteinModelPortaliP69922.
    SMRiP69922. Positions 1-591.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP69922.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the L-fucose isomerase family.Curated

    Phylogenomic databases

    eggNOGiCOG2407.
    HOGENOMiHOG000249674.
    InParanoidiP69922.
    KOiK01818.
    OMAiWGANHCV.
    OrthoDBiEOG6FJNCF.
    PhylomeDBiP69922.

    Family and domain databases

    Gene3Di3.20.14.10. 1 hit.
    3.40.275.10. 1 hit.
    3.40.50.1070. 1 hit.
    HAMAPiMF_01254. Fucose_iso.
    InterProiIPR004216. Fuc/Ara_isomerase_C.
    IPR015888. Fuc_isomerase_C.
    IPR012888. Fucose_iso_N1.
    IPR005763. Fucose_isomerase.
    IPR009015. Fucose_isomerase_N/cen.
    IPR012889. Fucose_isomerase_N2.
    [Graphical view]
    PfamiPF02952. Fucose_iso_C. 1 hit.
    PF07881. Fucose_iso_N1. 1 hit.
    PF07882. Fucose_iso_N2. 1 hit.
    [Graphical view]
    SUPFAMiSSF50443. SSF50443. 1 hit.
    SSF53743. SSF53743. 1 hit.
    TIGRFAMsiTIGR01089. fucI. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P69922-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKKISLPKIG IRPVIDGRRM GVRESLEEQT MNMAKATAAL LTEKLRHACG
    60 70 80 90 100
    AAVECVISDT CIAGMAEAAA CEEKFSSQNV GLTITVTPCW CYGSETIDMD
    110 120 130 140 150
    PTRPKAIWGF NGTERPGAVY LAAALAAHSQ KGIPAFSIYG HDVQDADDTS
    160 170 180 190 200
    IPADVEEKLL RFARAGLAVA SMKGKSYLSL GGVSMGIAGS IVDHNFFESW
    210 220 230 240 250
    LGMKVQAVDM TELRRRIDQK IYDEAELEMA LAWADKNFRY GEDENNKQYQ
    260 270 280 290 300
    RNAEQSRAVL RESLLMAMCI RDMMQGNSKL ADIGRVEESL GYNAIAAGFQ
    310 320 330 340 350
    GQRHWTDQYP NGDTAEAILN SSFDWNGVRE PFVVATENDS LNGVAMLMGH
    360 370 380 390 400
    QLTGTAQVFA DVRTYWSPEA IERVTGHKLD GLAEHGIIHL INSGSAALDG
    410 420 430 440 450
    SCKQRDSEGN PTMKPHWEIS QQEADACLAA TEWCPAIHEY FRGGGYSSRF
    460 470 480 490 500
    LTEGGVPFTM TRVNIIKGLG PVLQIAEGWS VELPKDVHDI LNKRTNSTWP
    510 520 530 540 550
    TTWFAPRLTG KGPFTDVYSV MANWGANHGV LTIGHVGADF ITLASMLRIP
    560 570 580 590
    VCMHNVEETK VYRPSAWAAH GMDIEGQDYR ACQNYGPLYK R
    Length:591
    Mass (Da):64,977
    Last modified:January 4, 2005 - v1
    Checksum:iE6245DEEDF34EF9B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81K → P AA sequence (PubMed:8052131).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X15025 Genomic DNA. Translation: CAA33127.1.
    U29581 Genomic DNA. Translation: AAB40452.1.
    U00096 Genomic DNA. Translation: AAC75844.1.
    AP009048 Genomic DNA. Translation: BAE76874.1.
    PIRiJS0185. ISECFI.
    RefSeqiNP_417282.1. NC_000913.3.
    WP_000724153.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75844; AAC75844; b2802.
    BAE76874; BAE76874; BAE76874.
    GeneIDi946195.
    KEGGieco:b2802.
    PATRICi32121020. VBIEscCol129921_2902.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X15025 Genomic DNA. Translation: CAA33127.1.
    U29581 Genomic DNA. Translation: AAB40452.1.
    U00096 Genomic DNA. Translation: AAC75844.1.
    AP009048 Genomic DNA. Translation: BAE76874.1.
    PIRiJS0185. ISECFI.
    RefSeqiNP_417282.1. NC_000913.3.
    WP_000724153.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FUIX-ray2.50A/B/C/D/E/F1-591[»]
    ProteinModelPortaliP69922.
    SMRiP69922. Positions 1-591.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP69922. 2 interactions.
    STRINGi511145.b2802.

    Proteomic databases

    PaxDbiP69922.
    PRIDEiP69922.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75844; AAC75844; b2802.
    BAE76874; BAE76874; BAE76874.
    GeneIDi946195.
    KEGGieco:b2802.
    PATRICi32121020. VBIEscCol129921_2902.

    Organism-specific databases

    EchoBASEiEB0345.
    EcoGeneiEG10349. fucI.

    Phylogenomic databases

    eggNOGiCOG2407.
    HOGENOMiHOG000249674.
    InParanoidiP69922.
    KOiK01818.
    OMAiWGANHCV.
    OrthoDBiEOG6FJNCF.
    PhylomeDBiP69922.

    Enzyme and pathway databases

    UniPathwayiUPA00563; UER00624.
    BioCyciEcoCyc:FUCISOM-MONOMER.
    ECOL316407:JW2773-MONOMER.
    MetaCyc:FUCISOM-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP69922.
    PROiP69922.

    Family and domain databases

    Gene3Di3.20.14.10. 1 hit.
    3.40.275.10. 1 hit.
    3.40.50.1070. 1 hit.
    HAMAPiMF_01254. Fucose_iso.
    InterProiIPR004216. Fuc/Ara_isomerase_C.
    IPR015888. Fuc_isomerase_C.
    IPR012888. Fucose_iso_N1.
    IPR005763. Fucose_isomerase.
    IPR009015. Fucose_isomerase_N/cen.
    IPR012889. Fucose_isomerase_N2.
    [Graphical view]
    PfamiPF02952. Fucose_iso_C. 1 hit.
    PF07881. Fucose_iso_N1. 1 hit.
    PF07882. Fucose_iso_N2. 1 hit.
    [Graphical view]
    SUPFAMiSSF50443. SSF50443. 1 hit.
    SSF53743. SSF53743. 1 hit.
    TIGRFAMsiTIGR01089. fucI. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation."
      Lu Z., Lin E.C.C.
      Nucleic Acids Res. 17:4883-4884(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Identification of a novel sugar-H+ symport protein, FucP, for transport of L-fucose into Escherichia coli."
      Gunn F.J., Tate C.G., Henderson P.J.F.
      Mol. Microbiol. 12:799-809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-9.
    5. "Enzymatic conversion of L-fucose to L-fuculose."
      Green M., Cohen S.S.
      J. Biol. Chem. 219:557-568(1956) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "Structure and mechanism of L-fucose isomerase from Escherichia coli."
      Seemann J.E., Schulz G.E.
      J. Mol. Biol. 273:256-268(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH L-FUCITOL, ACTIVE SITES, CATALYTIC ACTIVITY, REACTION MECHANISM.

    Entry informationi

    Entry nameiFUCI_ECOLI
    AccessioniPrimary (citable) accession number: P69922
    Secondary accession number(s): P11552, Q2MA32
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: January 4, 2005
    Last modified: July 22, 2015
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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

    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 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.