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Q5HES4

- FUMC_STAAC

UniProt

Q5HES4 - FUMC_STAAC

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Staphylococcus aureus (strain COL)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
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    • Comment

    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 sitei186 – 1861Proton donor/acceptorBy similarity
    Active sitei316 – 3161By similarity
    Binding sitei317 – 3171SubstrateUniRule annotation
    Sitei329 – 3291Important 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

    BioCyciSAUR93062:GCEP-1873-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
    Synonyms:citG
    Ordered Locus Names:SACOL1908
    OrganismiStaphylococcus aureus (strain COL)
    Taxonomic identifieri93062 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000000530: 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 – 461461Fumarate hydratase class IIPRO_0000161311Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi93062.SACOL1908.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5HES4.
    SMRiQ5HES4. Positions 3-457.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 993Substrate bindingUniRule annotation
    Regioni127 – 1304B siteUniRule annotation
    Regioni137 – 1393Substrate bindingUniRule annotation
    Regioni185 – 1862Substrate bindingUniRule annotation
    Regioni322 – 3243Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    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.

    Q5HES4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVRIEHDTF GEIEVPADKY WGAQTERSKR NFPVGKERMP IEVVYGFAQL    50
    KRAAAIANFD LGKLSEAKKD AIVYACDQIL SGELDEHFPL VVWQTGSGTQ 100
    SNMNVNEVVS YVANMYLKDH QSDESIHPND DVNKSQSSND TFPTAMHVAL 150
    YQEVETKLEP ALKLLRNTLK EKEDKFDSII KIGRTHLQDA TPIKLGQEIS 200
    GWRYMLDRCE TMLSESKKHI LNLAIGGTAV GTGINAHPEF GDKVAHYISE 250
    NTGYPFVSSE NKFHALTAHD EVVQLHGTLK ALAGDLMKIA NDVRWLASGP 300
    RAGLAEISIP ENEPGSSIMP GKVNPTQCEM LTMVAVQVMG NDTVVGFASS 350
    QGNFELNVYK PVIMHNTLQS IYLLADGMET FNNNCAVGIE PIEENIDNYL 400
    NQSLMLVTAL NPHIGYEKAA QIAKKAHKEG LTLKESAIQT GYVTEEQFEA 450
    WIKPEDMVDP H 461
    Length:461
    Mass (Da):51,108
    Last modified:February 15, 2005 - v1
    Checksum:iFA5B0EB76BBD4185
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000046 Genomic DNA. Translation: AAW36920.1.
    RefSeqiYP_186733.1. NC_002951.2.

    Genome annotation databases

    EnsemblBacteriaiAAW36920; AAW36920; SACOL1908.
    GeneIDi3237674.
    KEGGisac:SACOL1908.
    PATRICi19530033. VBIStaAur112458_1864.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000046 Genomic DNA. Translation: AAW36920.1 .
    RefSeqi YP_186733.1. NC_002951.2.

    3D structure databases

    ProteinModelPortali Q5HES4.
    SMRi Q5HES4. Positions 3-457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 93062.SACOL1908.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAW36920 ; AAW36920 ; SACOL1908 .
    GeneIDi 3237674.
    KEGGi sac:SACOL1908.
    PATRICi 19530033. VBIStaAur112458_1864.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    KOi K01679.
    OMAi MESFNIH.
    OrthoDBi EOG6V1M4M.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci SAUR93062:GCEP-1873-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. "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
      Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H.
      , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
      J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: COL.

    Entry informationi

    Entry nameiFUMC_STAAC
    AccessioniPrimary (citable) accession number: Q5HES4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 67 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

    Documents

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

    External Data

    Dasty 3