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Q60022

- FUMC_THEAQ

UniProt

Q60022 - FUMC_THEAQ

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Thermus aquaticus
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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

    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
    OrganismiThermus aquaticus
    Taxonomic identifieri271 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

    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 – 466466Fumarate hydratase class IIPRO_0000161326Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ60022.
    SMRiQ60022. Positions 4-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni99 – 1013Substrate 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

    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.

    Q60022-1 [UniParc]FASTAAdd to Basket

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    MEYRVERDTM GEVKVPADRY WGAQTQRSLE HFRIGAWRFR MPLEIIRAYG    50
    MLKKAAARAN LELGELPEEI ARAIIQAAEE VIAGKLDDHF PLVVFQTGSG 100
    TQTNMNVNEV IANRASEILG KPLGSKYVHP NDHVNRGQSS NDTFPTAMYV 150
    ATVLALHQHL YPAVEGLIAT FEEKARAFDG IVKVGRTHLM DAVPITLGQE 200
    VGSWAAQLRN TLAMVKEAEK GLYNLAIGGT AVGTGLNAHP RFGELVARYL 250
    AEETGLPFRV AENRFAALAA HDELVHVMGA LRTLAGALMK IGNDIRWLAS 300
    GPYGGIGEIF IPANEPGSSI MPGKVNPTQV EALPWVVVRV FGNDQAVAFA 350
    GSQGNFQLNV YKPVMVDAAL ESIKLLGDAV ASFDQHLAQG IEPNLERIEE 400
    HLNKNPMLAT ALNKAIGYDK AAEIVKKAIK EKKSLKQAAL ELGYLTEEEF 450
    DRIVVPMRLA KPHENA 466
    Length:466
    Mass (Da):50,954
    Last modified:November 1, 1996 - v1
    Checksum:iDC377E4A43D10284
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84646 Genomic DNA. Translation: BAA12702.1.
    PIRiT45269.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84646 Genomic DNA. Translation: BAA12702.1 .
    PIRi T45269.

    3D structure databases

    ProteinModelPortali Q60022.
    SMRi Q60022. Positions 4-463.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .

    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. "Cloning and nucleotide sequencing of genes encoding Mn-superoxide dismutase and class II fumarase from Thermus aquaticus YT-1."
      Motoshima H., Minagawa E., Tsukasaki F., Kaminogawa S.
      J. Ferment. Bioeng. 86:21-27(1998)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: YT1.

    Entry informationi

    Entry nameiFUMC_THEAQ
    AccessioniPrimary (citable) accession number: Q60022
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 70 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

    Documents

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

    External Data

    Dasty 3