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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

    Pathwayi: L-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)DescriptionActionsGraphical viewLength
    Active sitei337Proton acceptor1 Publication1
    Metal bindingi337Manganese1
    Active sitei361Proton acceptor1 Publication1
    Metal bindingi361Manganese1
    Metal bindingi528Manganese1

    GO - Molecular functioni

    • arabinose isomerase activity Source: EcoCyc
    • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 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)DescriptionActionsGraphical viewLength
    ChainiPRO_00002041451 – 591L-fucose isomeraseAdd BLAST591

    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

    BioGridi4259466. 6 interactors.
    IntActiP69922. 2 interactors.
    STRINGi511145.b2802.

    Structurei

    Secondary structure

    1591
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi8 – 14Combined sources7
    Turni19 – 21Combined sources3
    Helixi22 – 44Combined sources23
    Beta strandi55 – 57Combined sources3
    Helixi65 – 76Combined sources12
    Turni77 – 79Combined sources3
    Beta strandi80 – 89Combined sources10
    Helixi93 – 96Combined sources4
    Beta strandi101 – 103Combined sources3
    Beta strandi105 – 109Combined sources5
    Beta strandi113 – 115Combined sources3
    Helixi117 – 130Combined sources14
    Beta strandi136 – 138Combined sources3
    Helixi153 – 172Combined sources20
    Beta strandi176 – 182Combined sources7
    Helixi188 – 190Combined sources3
    Helixi194 – 201Combined sources8
    Beta strandi204 – 208Combined sources5
    Helixi211 – 218Combined sources8
    Helixi224 – 237Combined sources14
    Helixi247 – 249Combined sources3
    Helixi253 – 275Combined sources23
    Helixi279 – 282Combined sources4
    Helixi286 – 289Combined sources4
    Beta strandi294 – 299Combined sources6
    Turni302 – 308Combined sources7
    Helixi313 – 320Combined sources8
    Beta strandi321 – 324Combined sources4
    Beta strandi334 – 336Combined sources3
    Helixi340 – 353Combined sources14
    Beta strandi358 – 366Combined sources9
    Helixi368 – 375Combined sources8
    Helixi381 – 385Combined sources5
    Beta strandi387 – 390Combined sources4
    Helixi398 – 401Combined sources4
    Helixi416 – 418Combined sources3
    Helixi421 – 429Combined sources9
    Beta strandi432 – 435Combined sources4
    Turni438 – 440Combined sources3
    Beta strandi446 – 449Combined sources4
    Beta strandi457 – 466Combined sources10
    Turni467 – 469Combined sources3
    Beta strandi470 – 480Combined sources11
    Helixi485 – 494Combined sources10
    Beta strandi501 – 506Combined sources6
    Helixi512 – 514Combined sources3
    Helixi517 – 522Combined sources6
    Beta strandi525 – 534Combined sources10
    Helixi537 – 547Combined sources11
    Beta strandi551 – 553Combined sources3
    Helixi558 – 560Combined sources3
    Helixi566 – 569Combined sources4
    Helixi574 – 585Combined sources12

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP69922.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the L-fucose isomerase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105EHF. Bacteria.
    COG2407. LUCA.
    HOGENOMiHOG000249674.
    InParanoidiP69922.
    KOiK01818.
    OMAiGAISYGH.
    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. 1 hit.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti8K → P AA sequence (PubMed:8052131).Curated1

    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_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75844; AAC75844; b2802.
    BAE76874; BAE76874; BAE76874.
    GeneIDi946195.
    KEGGiecj:JW2773.
    eco: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_LN832404.1.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi4259466. 6 interactors.
    IntActiP69922. 2 interactors.
    STRINGi511145.b2802.

    Proteomic databases

    PaxDbiP69922.
    PRIDEiP69922.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75844; AAC75844; b2802.
    BAE76874; BAE76874; BAE76874.
    GeneIDi946195.
    KEGGiecj:JW2773.
    eco:b2802.
    PATRICi32121020. VBIEscCol129921_2902.

    Organism-specific databases

    EchoBASEiEB0345.
    EcoGeneiEG10349. fucI.

    Phylogenomic databases

    eggNOGiENOG4105EHF. Bacteria.
    COG2407. LUCA.
    HOGENOMiHOG000249674.
    InParanoidiP69922.
    KOiK01818.
    OMAiGAISYGH.
    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. 1 hit.
    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...

    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: November 2, 2016
    This is version 97 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

    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.