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Q9PL64

- FUMC_CHLMU

UniProt

Q9PL64 - FUMC_CHLMU

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Chlamydia muridarum (strain MoPn / Nigg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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

    BioCyciCMUR243161:GHYU-257-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:TC_0244
    OrganismiChlamydia muridarum (strain MoPn / Nigg)
    Taxonomic identifieri243161 [NCBI]
    Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
    ProteomesiUP000000800: 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 – 463463Fumarate hydratase class IIPRO_0000161267Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi243161.TC0244.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9PL64.
    SMRiQ9PL64. Positions 1-455.
    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.

    Q9PL64-1 [UniParc]FASTAAdd to Basket

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    MRQENDSLGI VMVPEDKLFG AQTGRSKNFF SYGKELMPIE VIQALVKIKK    50
    CAAKANGDLQ CLDAKRRDMI VAASDEILSG GLEEHFPLKV WQTGSGTQSN 100
    MNVNEVIANL AIKRHGGELG SKNPVHPNDH VNKSQSSNDV FPTAMHIAAV 150
    QSIKGSLIPA LEHLQKNLDA KALEFSRDIK IGRTHLMDAV PMTLGQEFSG 200
    YSHQLRSCLE RIGFSLTHLY ELAIGGTAVG TGLNVPEGFV DKVIYYLRQE 250
    TGEPFIPASN YFAALSNHDA LVQAHGSLAV LACSLIKIAT DLSFLGSGPR 300
    CGLGEIFFPE NEPGSSIMPG KINPTQSEAL QMVCSQVIGN NQSVIFSGTK 350
    GNFELNVMKP VIIYDFLQSV NLLSGAMRSF ADYFVSGLKV NRGQLQQNVE 400
    RSLMLVTALA PVLGYDKCSK IALKAFHENL SLKEACVSLG FLSEQEFDTH 450
    VVPGLMLGKR ERE 463
    Length:463
    Mass (Da):50,428
    Last modified:October 1, 2000 - v1
    Checksum:i7F3C5EA2F2991332
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002160 Genomic DNA. Translation: AAF39114.1.
    PIRiB81725.
    RefSeqiNP_296623.1. NC_002620.2.

    Genome annotation databases

    EnsemblBacteriaiAAF39114; AAF39114; TC_0244.
    GeneIDi1246413.
    KEGGicmu:TC_0244.
    PATRICi20371880. VBIChlMur19118_0267.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE002160 Genomic DNA. Translation: AAF39114.1 .
    PIRi B81725.
    RefSeqi NP_296623.1. NC_002620.2.

    3D structure databases

    ProteinModelPortali Q9PL64.
    SMRi Q9PL64. Positions 1-455.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243161.TC0244.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF39114 ; AAF39114 ; TC_0244 .
    GeneIDi 1246413.
    KEGGi cmu:TC_0244.
    PATRICi 20371880. VBIChlMur19118_0267.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci CMUR243161:GHYU-257-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: MoPn / Nigg.

    Entry informationi

    Entry nameiFUMC_CHLMU
    AccessioniPrimary (citable) accession number: Q9PL64
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 84 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