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Q822D5

- FUMC_CHLCV

UniProt

Q822D5 - FUMC_CHLCV

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Chlamydophila caviae (strain GPIC)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Jun 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

    BioCyciCCAV227941:GH8L-778-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:CCA_00748
    OrganismiChlamydophila caviae (strain GPIC)
    Taxonomic identifieri227941 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila
    ProteomesiUP000002193: 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 – 460460Fumarate hydratase class IIPRO_0000161266Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi227941.CCA00748.

    Structurei

    3D structure databases

    ProteinModelPortaliQ822D5.
    SMRiQ822D5. Positions 1-456.
    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.
    KOiK01679.
    OMAiAITNCEL.
    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.

    Q822D5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRQENDSLGI VEVPEDKLYG AQTARSQKYF SWAPEVMPKE VIRALVLIKQ    50
    CAAKANHDLG FLDSKYCDMI VSAASEILEG GFEEHFPLKV WQTGSGTQSN 100
    MNVNEVIANL AIQRHGGVVG SKTPIHPNDH VNKSQSSNDV FPTAMHIAAV 150
    INLKKKLIPA MDHLQRALDA KVAEFRDCVK IGRTHLMDAV PMTLGQEFSG 200
    YSNQIRQSLE RVAFSLTHMY ELAIGGTAVG TGLNVPNGFI DKVIHYLRQE 250
    TGEPFVAASN YFSALSNHDT LVNAHGVLAT LACALTKIAT DLSFLGSGPR 300
    CGLGELLFPE NEPGSSIMPG KINPTQCEAL QMVCAQVIGN NQAVIMGGSR 350
    GNFELNVMKP VIIYNFLQSV DILAGGMQAF ADYFVSGLRV NKPRLKEYLD 400
    NSLMLVTALT PVLGYDKCSK MALKAFHDNI NLKEACIQMG YLSAEEFDRL 450
    VVPESMVGKF 460
    Length:460
    Mass (Da):50,259
    Last modified:June 1, 2003 - v1
    Checksum:i8F68DE2F0046AFDA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015925 Genomic DNA. Translation: AAP05489.1.
    RefSeqiNP_829611.1. NC_003361.3.
    WP_011006703.1. NC_003361.3.

    Genome annotation databases

    EnsemblBacteriaiAAP05489; AAP05489; CCA_00748.
    GeneIDi1218433.
    KEGGicca:CCA00748.
    PATRICi20270625. VBIChlCav107360_0795.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015925 Genomic DNA. Translation: AAP05489.1 .
    RefSeqi NP_829611.1. NC_003361.3.
    WP_011006703.1. NC_003361.3.

    3D structure databases

    ProteinModelPortali Q822D5.
    SMRi Q822D5. Positions 1-456.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 227941.CCA00748.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP05489 ; AAP05489 ; CCA_00748 .
    GeneIDi 1218433.
    KEGGi cca:CCA00748.
    PATRICi 20270625. VBIChlCav107360_0795.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci CCAV227941:GH8L-778-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. "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
      Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G.
      , Rank R.G., Bavoil P.M., Fraser C.M.
      Nucleic Acids Res. 31:2134-2147(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: GPIC.

    Entry informationi

    Entry nameiFUMC_CHLCV
    AccessioniPrimary (citable) accession number: Q822D5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 77 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