Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

L-fuconate dehydratase

Gene

XCC4069

Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the catabolism of L-fucose. Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion. L-fuconate is the preferred substrate with 15-fold lower activity observed for L-galactonate and 8-fold lower activity with D-arabinonate. No activity detected with D-fuconate. Can also catalyze the epimerization of L-talonate and D-ribonate, but at slow rates.1 Publication

Catalytic activityi

L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H2O.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Kineticsi

  1. KM=0.03 mM for L-fuconate1 Publication
  2. KM=6.2 mM for L-galactonate1 Publication
  3. KM=2.1 mM for D-arabinonate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei32Substrate1 Publication1
    Binding sitei218Substrate1 Publication1
    Active sitei220Proton donor/acceptor1 Publication1
    Metal bindingi248Magnesium2 Publications1
    Binding sitei250Substrate1 Publication1
    Metal bindingi274Magnesium2 Publications1
    Binding sitei274Substrate1 Publication1
    Metal bindingi301Magnesium2 Publications1
    Binding sitei301Substrate1 Publication1
    Active sitei351Sequence analysis1
    Binding sitei382Substrate1 Publication1

    GO - Molecular functioni

    • L-fuconate dehydratase activity Source: UniProtKB
    • magnesium ion binding Source: UniProtKB

    GO - Biological processi

    • carbohydrate catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciXCAM190485:GIXZ-4066-MONOMER.
    SABIO-RKQ8P3K2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-fuconate dehydratase1 Publication (EC:4.2.1.681 Publication1 Publication)
    Short name:
    FucD1 Publication
    Gene namesi
    Ordered Locus Names:XCC4069
    OrganismiXanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
    Taxonomic identifieri190485 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
    Proteomesi
    • UP000001010 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi220K → A: Inactive. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004188131 – 441L-fuconate dehydrataseAdd BLAST441

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    STRINGi190485.XCC4069.

    Structurei

    Secondary structure

    1441
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 13Combined sources11
    Helixi16 – 18Combined sources3
    Turni19 – 22Combined sources4
    Beta strandi33 – 43Combined sources11
    Beta strandi48 – 55Combined sources8
    Helixi60 – 68Combined sources9
    Helixi71 – 74Combined sources4
    Helixi79 – 84Combined sources6
    Helixi86 – 94Combined sources9
    Helixi97 – 101Combined sources5
    Beta strandi104 – 106Combined sources3
    Helixi107 – 127Combined sources21
    Helixi132 – 137Combined sources6
    Helixi141 – 147Combined sources7
    Turni154 – 156Combined sources3
    Helixi159 – 169Combined sources11
    Helixi170 – 172Combined sources3
    Helixi173 – 183Combined sources11
    Beta strandi185 – 193Combined sources9
    Helixi199 – 211Combined sources13
    Beta strandi215 – 220Combined sources6
    Helixi225 – 239Combined sources15
    Beta strandi241 – 248Combined sources8
    Helixi255 – 263Combined sources9
    Helixi266 – 268Combined sources3
    Beta strandi270 – 274Combined sources5
    Helixi282 – 292Combined sources11
    Beta strandi297 – 299Combined sources3
    Helixi306 – 315Combined sources10
    Beta strandi319 – 321Combined sources3
    Turni325 – 327Combined sources3
    Helixi330 – 343Combined sources14
    Turni354 – 356Combined sources3
    Helixi357 – 371Combined sources15
    Beta strandi381 – 383Combined sources3
    Helixi388 – 390Combined sources3
    Beta strandi391 – 393Combined sources3
    Beta strandi397 – 402Combined sources6
    Beta strandi407 – 409Combined sources3
    Helixi416 – 422Combined sources7
    Turni424 – 426Combined sources3
    Helixi428 – 434Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1YEYX-ray2.34A/B/C/D1-441[»]
    2HNEX-ray2.00A/B/C/D1-436[»]
    2HXTX-ray1.70A1-441[»]
    2HXUX-ray1.80A1-441[»]
    ProteinModelPortaliQ8P3K2.
    SMRiQ8P3K2.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8P3K2.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni22 – 24Substrate binding1 Publication3
    Regioni351 – 353Substrate binding1 Publication3

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105DIA. Bacteria.
    COG4948. LUCA.
    HOGENOMiHOG000113757.
    KOiK18334.
    OMAiSAAYCIL.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProiIPR029065. Enolase_C-like.
    IPR029017. Enolase_N-like.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N_dom.
    IPR001354. MR/MLE/MAL.
    [Graphical view]
    PANTHERiPTHR13794. PTHR13794. 2 hits.
    PfamiPF13378. MR_MLE_C. 1 hit.
    PF02746. MR_MLE_N. 1 hit.
    [Graphical view]
    SMARTiSM00922. MR_MLE. 1 hit.
    [Graphical view]
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8P3K2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRTIIALETH DVRFPTSREL DGSDAMNPDP DYSAAYVVLR TDGAEDLAGY
    60 70 80 90 100
    GLVFTIGRGN DVQTAAVAAL AEHVVGLSVD KVIADLGAFA RRLTNDSQLR
    110 120 130 140 150
    WLGPEKGVMH MAIGAVINAA WDLAARAANK PLWRFIAELT PEQLVDTIDF
    160 170 180 190 200
    RYLSDALTRD EALAILRDAQ PQRAARTATL IEQGYPAYTT SPGWLGYSDE
    210 220 230 240 250
    KLVRLAKEAV ADGFRTIKLK VGANVQDDIR RCRLARAAIG PDIAMAVDAN
    260 270 280 290 300
    QRWDVGPAID WMRQLAEFDI AWIEEPTSPD DVLGHAAIRQ GITPVPVSTG
    310 320 330 340 350
    EHTQNRVVFK QLLQAGAVDL IQIDAARVGG VNENLAILLL AAKFGVRVFP
    360 370 380 390 400
    HAGGVGLCEL VQHLAMADFV AITGKMEDRA IEFVDHLHQH FLDPVRIQHG
    410 420 430 440
    RYLAPEVPGF SAEMHPASIA EFSYPDGRFW VEDLAASKAK A
    Length:441
    Mass (Da):48,124
    Last modified:October 1, 2002 - v1
    Checksum:i4BAF5BEC1D1E3327
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE008922 Genomic DNA. Translation: AAM43290.1.
    RefSeqiNP_639408.1. NC_003902.1.
    WP_011039138.1. NC_003902.1.

    Genome annotation databases

    EnsemblBacteriaiAAM43290; AAM43290; XCC4069.
    GeneIDi1000844.
    KEGGixcc:XCC4069.
    PATRICi24079370. VBIXanCam115730_4361.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE008922 Genomic DNA. Translation: AAM43290.1.
    RefSeqiNP_639408.1. NC_003902.1.
    WP_011039138.1. NC_003902.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1YEYX-ray2.34A/B/C/D1-441[»]
    2HNEX-ray2.00A/B/C/D1-436[»]
    2HXTX-ray1.70A1-441[»]
    2HXUX-ray1.80A1-441[»]
    ProteinModelPortaliQ8P3K2.
    SMRiQ8P3K2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi190485.XCC4069.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAM43290; AAM43290; XCC4069.
    GeneIDi1000844.
    KEGGixcc:XCC4069.
    PATRICi24079370. VBIXanCam115730_4361.

    Phylogenomic databases

    eggNOGiENOG4105DIA. Bacteria.
    COG4948. LUCA.
    HOGENOMiHOG000113757.
    KOiK18334.
    OMAiSAAYCIL.

    Enzyme and pathway databases

    BioCyciXCAM190485:GIXZ-4066-MONOMER.
    SABIO-RKQ8P3K2.

    Miscellaneous databases

    EvolutionaryTraceiQ8P3K2.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProiIPR029065. Enolase_C-like.
    IPR029017. Enolase_N-like.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N_dom.
    IPR001354. MR/MLE/MAL.
    [Graphical view]
    PANTHERiPTHR13794. PTHR13794. 2 hits.
    PfamiPF13378. MR_MLE_C. 1 hit.
    PF02746. MR_MLE_N. 1 hit.
    [Graphical view]
    SMARTiSM00922. MR_MLE. 1 hit.
    [Graphical view]
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiFUCD_XANCP
    AccessioniPrimary (citable) accession number: Q8P3K2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: October 1, 2002
    Last modified: November 2, 2016
    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, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.