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Q7VKC9

- FUMC_HAEDU

UniProt

Q7VKC9 - FUMC_HAEDU

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible addition of water to fumarate to give L-malate.By similarity

    Catalytic activityi

    (S)-malate = fumarate + H2O.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei188 – 1881Proton donor/acceptorBy similarity
    Active sitei318 – 3181By similarity
    Binding sitei319 – 3191SubstrateUniRule annotation
    Sitei331 – 3311Important for catalytic activityBy similarity

    GO - Molecular functioni

    1. fumarate hydratase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. fumarate metabolic process Source: InterPro
    2. tricarboxylic acid cycle Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciHDUC233412:GH5F-1794-MONOMER.
    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase class IIUniRule annotation (EC:4.2.1.2UniRule annotation)
    Short name:
    Fumarase CUniRule annotation
    Gene namesi
    Name:fumCUniRule annotation
    Ordered Locus Names:HD_1986
    OrganismiHaemophilus ducreyi (strain 35000HP / ATCC 700724)
    Taxonomic identifieri233412 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000001022: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. tricarboxylic acid cycle enzyme complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 464464Fumarate hydratase class IIPRO_0000161278Add
    BLAST

    Proteomic databases

    PRIDEiQ7VKC9.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi233412.HD1986.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7VKC9.
    SMRiQ7VKC9. Positions 4-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni98 – 1003Substrate bindingUniRule annotation
    Regioni129 – 1324B siteUniRule annotation
    Regioni139 – 1413Substrate bindingUniRule annotation
    Regioni187 – 1882Substrate bindingUniRule annotation
    Regioni324 – 3263Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0114.
    KOiK01679.
    OMAiMESFNIH.
    OrthoDBiEOG6V1M4M.

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    HAMAPiMF_00743. FumaraseC.
    InterProiIPR005677. Fum_hydII.
    IPR024083. Fumarase/histidase_N.
    IPR018951. Fumarase_C_C.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    [Graphical view]
    PANTHERiPTHR11444. PTHR11444. 1 hit.
    PfamiPF10415. FumaraseC_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view]
    PRINTSiPR00149. FUMRATELYASE.
    SUPFAMiSSF48557. SSF48557. 1 hit.
    TIGRFAMsiTIGR00979. fumC_II. 1 hit.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7VKC9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEYRIEKDTM GEVKVPADRY WAAQTERSRN NFRIGPEASM PVEIIEAFAY    50
    LKKAAAFANA ELGALTTEKR DLIAMVCDEI LANKLADEFP LVIWQTGSGT 100
    QSNMNLNEVI ANRAHVLQGG ALGEKSIIHP NDDVNKSQSS NDTYPTAMHI 150
    AAYKKVVEVT IPAIERLQKT FAIKSEAFKD VVKIGRTHLM DATPLTLGQE 200
    FSAYAAQLQF GLLALKNTLP HLAQLALGGT AVGTGLNTPK GYDVKVAEYI 250
    AQFTQLPFIT AENKFEALAT HDAIIETHGA LKQIAMSLFK IANDIRLLAS 300
    GPRSGIGEIL IPENEPGSSI MPGKVNPTQC EAMTMVAAQV LGNDTTISFA 350
    GSQGHFQLNV FKPVMAANFL QSAQLLADVC ISFDEHCASG IEPNYPRIQQ 400
    QLENSLMLVT ALNTHIGYEN AAKIAKTAHK NGTTLKEEAI NLGLVTAEQF 450
    DQWVRPQNMV GSLK 464
    Length:464
    Mass (Da):50,483
    Last modified:October 1, 2003 - v1
    Checksum:i7FC2E242353C1DEC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017143 Genomic DNA. Translation: AAP96703.1.
    RefSeqiNP_874314.1. NC_002940.2.

    Genome annotation databases

    EnsemblBacteriaiAAP96703; AAP96703; HD_1986.
    GeneIDi1491818.
    KEGGihdu:HD1986.
    PATRICi20180098. VBIHaeDuc133973_1664.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017143 Genomic DNA. Translation: AAP96703.1 .
    RefSeqi NP_874314.1. NC_002940.2.

    3D structure databases

    ProteinModelPortali Q7VKC9.
    SMRi Q7VKC9. Positions 4-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 233412.HD1986.

    Proteomic databases

    PRIDEi Q7VKC9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP96703 ; AAP96703 ; HD_1986 .
    GeneIDi 1491818.
    KEGGi hdu:HD1986.
    PATRICi 20180098. VBIHaeDuc133973_1664.

    Phylogenomic databases

    eggNOGi COG0114.
    KOi K01679.
    OMAi MESFNIH.
    OrthoDBi EOG6V1M4M.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci HDUC233412:GH5F-1794-MONOMER.

    Family and domain databases

    Gene3Di 1.10.275.10. 1 hit.
    HAMAPi MF_00743. FumaraseC.
    InterProi IPR005677. Fum_hydII.
    IPR024083. Fumarase/histidase_N.
    IPR018951. Fumarase_C_C.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    [Graphical view ]
    PANTHERi PTHR11444. PTHR11444. 1 hit.
    Pfami PF10415. FumaraseC_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00149. FUMRATELYASE.
    SUPFAMi SSF48557. SSF48557. 1 hit.
    TIGRFAMsi TIGR00979. fumC_II. 1 hit.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of Haemophilus ducreyi."
      Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 35000HP / ATCC 700724.

    Entry informationi

    Entry nameiFUMC_HAEDU
    AccessioniPrimary (citable) accession number: Q7VKC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors By similarity.By similarity

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3