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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: -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

    Keywordsi

    Molecular functionLyase
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciXCAM190485:G1FZM-4067-MONOMER
    SABIO-RKiQ8P3K2

    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
    OMAiLVSCIDF

    Family and domain databases

    CDDicd03324 rTSbeta_L-fuconate_dehydratase, 1 hit
    Gene3Di3.20.20.120, 1 hit
    3.30.390.10, 1 hit
    InterProiView protein in InterPro
    IPR036849 Enolase-like_C_sf
    IPR029017 Enolase-like_N
    IPR034390 Enolase-like_superfamily
    IPR029065 Enolase_C-like
    IPR034610 L-fuconate_dehydratase
    IPR034593 Mandelate_racemase-like
    IPR013342 Mandelate_racemase_C
    IPR013341 Mandelate_racemase_N_dom
    PANTHERiPTHR13794:SF58 PTHR13794:SF58, 1 hit
    PfamiView protein in Pfam
    PF13378 MR_MLE_C, 1 hit
    PF02746 MR_MLE_N, 1 hit
    SFLDiSFLDF00111 L-fuconate_dehydratase, 1 hit
    SFLDG00179 mandelate_racemase, 1 hit
    SFLDS00001 Enolase, 1 hit
    SMARTiView protein in SMART
    SM00922 MR_MLE, 1 hit
    SUPFAMiSSF51604 SSF51604, 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
    35547718
    KEGGixcc:XCC4069
    PATRICifig|190485.4.peg.4361

    Similar proteinsi

    Entry informationi

    Entry nameiFUCD_XANCP
    AccessioniPrimary (citable) accession number: Q8P3K2
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: October 1, 2002
    Last modified: March 28, 2018
    This is version 94 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health