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Q83CL8

- FUMC_COXBU

UniProt

Q83CL8 - FUMC_COXBU

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 2 (15 Dec 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 sitei185 – 1851Proton donor/acceptorBy similarity
    Active sitei315 – 3151By similarity
    Binding sitei316 – 3161SubstrateUniRule annotation
    Sitei328 – 3281Important 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

    BioCyciCBUR227377:GJ7S-1090-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:CBU_1096
    OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
    Taxonomic identifieri227377 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
    ProteomesiUP000002671: 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 – 459459Fumarate hydratase class IIPRO_0000161273Add
    BLAST

    Proteomic databases

    PRIDEiQ83CL8.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi227377.CBU_1096.

    Structurei

    3D structure databases

    ProteinModelPortaliQ83CL8.
    SMRiQ83CL8. Positions 1-457.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni95 – 973Substrate bindingUniRule annotation
    Regioni126 – 1294B siteUniRule annotation
    Regioni136 – 1383Substrate bindingUniRule annotation
    Regioni184 – 1852Substrate bindingUniRule annotation
    Regioni321 – 3233Substrate 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.

    Q83CL8-1 [UniParc]FASTAAdd to Basket

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    MRKESDSMGT IEVPSEKYYG AQSQRSLINF AIGRETMPPE LIRAFGVLKK    50
    AAVLTNVELG KVSQEKANFI LKACEELIAG KLNDHFPLKI WQTGSGTQTN 100
    MNVNEVISNR AIELAGGKLG SKEPVHPNDH VNMSQSSNDT FPTAMHITAA 150
    EMITHQLIPN LTVLRDTLEK KSKEFSEIIK IGRTHLQDAV PLTLGQEFSG 200
    YVAQLNHNLE AINDVLPTLY RLALGGTAVG TGLNTHPQFA KKAADHIAEL 250
    TGIPFYSASN KFAALAANDE IVLVSGVLKT LACSLMKIAN DIRWLASGPR 300
    CGIGEIVIPE NEPGSSIMPG KVNPTQSEAM TMVCVQVIGN DTTITIAGSQ 350
    GNFELNVYKP VMAYNLIQSI YLLSDACRSF NDHCAVGIKP NQEKINDYLN 400
    NSLMLVTALN QIIGYDKASE IAKKAYKEGT TLKEAALQLG YLTASEFDKA 450
    VDPKKMVAI 459
    Length:459
    Mass (Da):49,850
    Last modified:December 15, 2003 - v2
    Checksum:i15153802D24B2359
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016828 Genomic DNA. Translation: AAO90609.2.
    RefSeqiNP_820095.2. NC_002971.3.

    Genome annotation databases

    EnsemblBacteriaiAAO90609; AAO90609; CBU_1096.
    GeneIDi1208998.
    KEGGicbu:CBU_1096.
    PATRICi17930925. VBICoxBur82552_1090.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016828 Genomic DNA. Translation: AAO90609.2 .
    RefSeqi NP_820095.2. NC_002971.3.

    3D structure databases

    ProteinModelPortali Q83CL8.
    SMRi Q83CL8. Positions 1-457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 227377.CBU_1096.

    Proteomic databases

    PRIDEi Q83CL8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO90609 ; AAO90609 ; CBU_1096 .
    GeneIDi 1208998.
    KEGGi cbu:CBU_1096.
    PATRICi 17930925. VBICoxBur82552_1090.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci CBUR227377:GJ7S-1090-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RSA 493 / Nine Mile phase I.

    Entry informationi

    Entry nameiFUMC_COXBU
    AccessioniPrimary (citable) accession number: Q83CL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 75 of the entry and version 2 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. Coxiella burnetii
      Coxiella burnetii (strain RSA 493): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3