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O66271

- FUMC_THET2

UniProt

O66271 - FUMC_THET2

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (24 May 2004)
      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 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

    BioCyciTTHE262724:GCAT-194-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:TT_C0190
    OrganismiThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
    Taxonomic identifieri262724 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000592: 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 – 466466Fumarate hydratase class IIPRO_0000161327Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi262724.TTC0190.

    Structurei

    3D structure databases

    ProteinModelPortaliO66271.
    SMRiO66271. 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

    Phylogenomic databases

    eggNOGiCOG0114.
    KOiK01679.
    OMAiGYLEAKI.
    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.

    O66271-1 [UniParc]FASTAAdd to Basket

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    MEYRIERDTM GEVRVPADKY WGAQTQRSLE NFRIGTDRFR MPLEIIRAYG    50
    MLKKAAARAN LELGELPEEI AKAIIQAAEE VVQGKWDDHF PLVVFQTGSG 100
    TQTNMNVNEV IANRASEILG KPLGSKYVHP NDHVNRGQSS NDTFPTAMYV 150
    AVALALHQRL YPAVEGLIRT FTAKAQAFDQ IVKVGRTHLM DAVPITLGQE 200
    IGSWAAQLKT TLAAVKEMEK GLYNLAIGGT AVGTGLNAHP RFGELVAKYL 250
    AEETGLPFRV AENRFAALAA HDELVNVMGA IRTLAGALMK IGNDVRWLAS 300
    GPYAGIGEIT IPANEPGSSI MPGKVNPTQV EALTMVVVRV YGNDHTVAFA 350
    GSQGNFQLNV YKPVMAYSTL ESINLLADAV ASFDAHLAQG IEPNLERIEE 400
    HLQKNPMLAT ALNKAIGYDK AAEIVKKALK EKKTLKQAAL ELGYLTEEEF 450
    DRIVVPMRLA KPHEGA 466
    Length:466
    Mass (Da):50,882
    Last modified:May 24, 2004 - v2
    Checksum:iC0ED1307333A65A8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341I → F in BAA25700. 1 PublicationCurated
    Sequence conflicti238 – 2381A → G in BAA25700. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB010884 Genomic DNA. Translation: BAA25700.1.
    AE017221 Genomic DNA. Translation: AAS80538.1.
    PIRiT43727.
    RefSeqiWP_011172644.1. NC_005835.1.
    YP_004165.1. NC_005835.1.

    Genome annotation databases

    EnsemblBacteriaiAAS80538; AAS80538; TT_C0190.
    GeneIDi2774678.
    KEGGitth:TTC0190.
    PATRICi23950773. VBITheThe54392_0191.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB010884 Genomic DNA. Translation: BAA25700.1 .
    AE017221 Genomic DNA. Translation: AAS80538.1 .
    PIRi T43727.
    RefSeqi WP_011172644.1. NC_005835.1.
    YP_004165.1. NC_005835.1.

    3D structure databases

    ProteinModelPortali O66271.
    SMRi O66271. Positions 4-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 262724.TTC0190.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS80538 ; AAS80538 ; TT_C0190 .
    GeneIDi 2774678.
    KEGGi tth:TTC0190.
    PATRICi 23950773. VBITheThe54392_0191.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci TTHE262724:GCAT-194-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. "Molecular cloning and sequence analysis of the fumC and sodA genes from an extremely thermophilic eubacterium Thermus thermophilus."
      Kosuge T., Umehara K., Matsuura S., Hoshino T.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB27 / ATCC BAA-163 / DSM 7039.

    Entry informationi

    Entry nameiFUMC_THET2
    AccessioniPrimary (citable) accession number: O66271
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: May 24, 2004
    Last modified: October 1, 2014
    This is version 90 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

    Documents

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

    External Data

    Dasty 3