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P69922

- FUCI_ECOLI

UniProt

P69922 - FUCI_ECOLI

Protein

L-fucose isomerase

Gene

fucI

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (04 Jan 2005)
      Previous versions | rss
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    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

    Manganese.

    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

    Pathwayi

    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

    1. arabinose isomerase activity Source: EcoCyc
    2. identical protein binding Source: IntAct
    3. L-fucose isomerase activity Source: EcoCyc
    4. manganese ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. D-arabinose catabolic process Source: EcoCyc
    2. L-fucose catabolic process Source: EcoCyc

    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10349. fucI.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    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.

    Gene expression databases

    GenevestigatoriP69922.

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK01818.
    OMAiKEGQDYR.
    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

    MKKISLPKIG IRPVIDGRRM GVRESLEEQT MNMAKATAAL LTEKLRHACG    50
    AAVECVISDT CIAGMAEAAA CEEKFSSQNV GLTITVTPCW CYGSETIDMD 100
    PTRPKAIWGF NGTERPGAVY LAAALAAHSQ KGIPAFSIYG HDVQDADDTS 150
    IPADVEEKLL RFARAGLAVA SMKGKSYLSL GGVSMGIAGS IVDHNFFESW 200
    LGMKVQAVDM TELRRRIDQK IYDEAELEMA LAWADKNFRY GEDENNKQYQ 250
    RNAEQSRAVL RESLLMAMCI RDMMQGNSKL ADIGRVEESL GYNAIAAGFQ 300
    GQRHWTDQYP NGDTAEAILN SSFDWNGVRE PFVVATENDS LNGVAMLMGH 350
    QLTGTAQVFA DVRTYWSPEA IERVTGHKLD GLAEHGIIHL INSGSAALDG 400
    SCKQRDSEGN PTMKPHWEIS QQEADACLAA TEWCPAIHEY FRGGGYSSRF 450
    LTEGGVPFTM TRVNIIKGLG PVLQIAEGWS VELPKDVHDI LNKRTNSTWP 500
    TTWFAPRLTG KGPFTDVYSV MANWGANHGV LTIGHVGADF ITLASMLRIP 550
    VCMHNVEETK VYRPSAWAAH GMDIEGQDYR ACQNYGPLYK R 591
    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:
    EMBL
    GenBank
    DDBJ
    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.
    YP_491010.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75844; AAC75844; b2802.
    BAE76874; BAE76874; BAE76874.
    GeneIDi12930472.
    946195.
    KEGGiecj:Y75_p2739.
    eco:b2802.
    PATRICi32121020. VBIEscCol129921_2902.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi JS0185. ISECFI.
    RefSeqi NP_417282.1. NC_000913.3.
    YP_491010.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FUI X-ray 2.50 A/B/C/D/E/F 1-591 [» ]
    ProteinModelPortali P69922.
    SMRi P69922. Positions 1-591.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P69922. 2 interactions.
    STRINGi 511145.b2802.

    Proteomic databases

    PaxDbi P69922.
    PRIDEi P69922.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75844 ; AAC75844 ; b2802 .
    BAE76874 ; BAE76874 ; BAE76874 .
    GeneIDi 12930472.
    946195.
    KEGGi ecj:Y75_p2739.
    eco:b2802.
    PATRICi 32121020. VBIEscCol129921_2902.

    Organism-specific databases

    EchoBASEi EB0345.
    EcoGenei EG10349. fucI.

    Phylogenomic databases

    eggNOGi COG2407.
    HOGENOMi HOG000249674.
    KOi K01818.
    OMAi KEGQDYR.
    OrthoDBi EOG6FJNCF.
    PhylomeDBi P69922.

    Enzyme and pathway databases

    UniPathwayi UPA00563 ; UER00624 .
    BioCyci EcoCyc:FUCISOM-MONOMER.
    ECOL316407:JW2773-MONOMER.
    MetaCyc:FUCISOM-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P69922.
    PROi P69922.

    Gene expression databases

    Genevestigatori P69922.

    Family and domain databases

    Gene3Di 3.20.14.10. 1 hit.
    3.40.275.10. 1 hit.
    3.40.50.1070. 1 hit.
    HAMAPi MF_01254. Fucose_iso.
    InterProi IPR004216. 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 ]
    Pfami PF02952. Fucose_iso_C. 1 hit.
    PF07881. Fucose_iso_N1. 1 hit.
    PF07882. Fucose_iso_N2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50443. SSF50443. 1 hit.
    SSF53743. SSF53743. 1 hit.
    TIGRFAMsi TIGR01089. fucI. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 86 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