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Q89XM2

- FUMC2_BRADU

UniProt

Q89XM2 - FUMC2_BRADU

Protein

Fumarate hydratase class II 2

Gene

fumC2

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 78 (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 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

    BioCyciBJAP224911:GJEJ-287-MONOMER.
    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase class II 2UniRule annotation (EC:4.2.1.2UniRule annotation)
    Short name:
    Fumarase C 2UniRule annotation
    Gene namesi
    Name:fumC2UniRule annotation
    Ordered Locus Names:bll0286
    OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
    Taxonomic identifieri224911 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
    ProteomesiUP000002526: 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 – 478478Fumarate hydratase class II 2PRO_0000161260Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi224911.bll0286.

    Structurei

    3D structure databases

    ProteinModelPortaliQ89XM2.
    SMRiQ89XM2. Positions 4-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni98 – 1003Substrate 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.
    HOGENOMiHOG000061736.
    KOiK01679.
    OrthoDBiEOG6V1M4M.
    PhylomeDBiQ89XM2.

    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.

    Q89XM2-1 [UniParc]FASTAAdd to Basket

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    MNDLRKETDS LGEVNVPADK LWGAQTQRSL EHFSIGRDLM PREMIQSYAI    50
    LKKAAANANY AGGRLDGKIH KLIVHTCDEI LAGQHHDMFP LHVWMTGSGT 100
    QFNMNVNEVI SNRCCQLAGT ALGSKLPVHP NDHVNMSQSS NDSFPSAMYI 150
    AAAMNVTQRL VPAVEALHDA IAAKSNQWDD IVKIGRTHMQ DATPLTLGQE 200
    WSGYAAMLAD GLARIDDALK GVFRLALGGT AVGTGINAAP GFAEAVAAEI 250
    ARLTGLPFVS APNKFAVQGA HDALVQLSGT LRTLAGSLYK IANDIRLLSC 300
    GPRAGFAELR IPENEPGSSI MPGKVNPTQA EALTMIAVQV MANDVAVGFG 350
    GAGGYLEMNV YKPLIIHNIA QSVTILTDGC TNFRTFLVEG TEPNRKKIKE 400
    YVERSLMLVT ALAPVIGYDK ASRIAHYAMD NDLTLKSAAL KLGFVTEPEF 450
    DRIVDPAKMV KPYVAEIKVP LAIGAKTG 478
    Length:478
    Mass (Da):51,299
    Last modified:December 15, 2003 - v2
    Checksum:iA33EC007B6A88B44
    GO

    Sequence cautioni

    The sequence BAC45551.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000040 Genomic DNA. Translation: BAC45551.1. Different initiation.
    RefSeqiNP_766926.2. NC_004463.1.

    Genome annotation databases

    EnsemblBacteriaiBAC45551; BAC45551; BAC45551.
    GeneIDi1048934.
    KEGGibja:bll0286.
    PATRICi21184003. VBIBraJap65052_0281.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000040 Genomic DNA. Translation: BAC45551.1 . Different initiation.
    RefSeqi NP_766926.2. NC_004463.1.

    3D structure databases

    ProteinModelPortali Q89XM2.
    SMRi Q89XM2. Positions 4-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224911.bll0286.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC45551 ; BAC45551 ; BAC45551 .
    GeneIDi 1048934.
    KEGGi bja:bll0286.
    PATRICi 21184003. VBIBraJap65052_0281.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    KOi K01679.
    OrthoDBi EOG6V1M4M.
    PhylomeDBi Q89XM2.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci BJAP224911:GJEJ-287-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: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

    Entry informationi

    Entry nameiFUMC2_BRADU
    AccessioniPrimary (citable) accession number: Q89XM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 78 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3