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Q9KCX4

- FUMC_BACHD

UniProt

Q9KCX4 - FUMC_BACHD

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (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 sitei186 – 1861Proton donor/acceptorBy similarity
    Active sitei316 – 3161By similarity
    Binding sitei317 – 3171SubstrateUniRule annotation
    Sitei329 – 3291Important 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

    BioCyciBHAL272558:GJC5-1528-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
    Synonyms:citG
    Ordered Locus Names:BH1445
    OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
    Taxonomic identifieri272558 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001258: 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 – 462462Fumarate hydratase class IIPRO_0000161254Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272558.BH1445.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9KCX4.
    SMRiQ9KCX4. Positions 4-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 993Substrate bindingUniRule annotation
    Regioni127 – 1304B siteUniRule annotation
    Regioni137 – 1393Substrate bindingUniRule annotation
    Regioni185 – 1862Substrate bindingUniRule annotation
    Regioni322 – 3243Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    KOiK01679.
    OMAiAARHMKL.
    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.

    Q9KCX4-1 [UniParc]FASTAAdd to Basket

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    MNTRIERDTL GEMHVPQDKL WGAQTQRSYE NFHIGTEKMP MEIIYAFALL    50
    KKAAANVNKK LGQLSAEKAD AITWAANEVL AGKHDDHFPL FVWQTGSGTQ 100
    SNMNMNEVLA RRGNQLLQEK GLDVTIHPND DVNRSQSSND TFPTAMHIAA 150
    YNKLDDHLLP TLQMFKQTLH QKAKQFDDVI KLGRTHLQDA TPLTLGQEIS 200
    GWARMLEKTE QMIRESMIYL QELAIGGTAV GTGVNAHPKF GEMVAADIAN 250
    ETGKPFKSAA NKFHALTSHD ELVHTHGALK ALAADLFKIA NDIRWLASGP 300
    RGGLGELIIP ANEPGSSIMP GKVNPTQSEA LTMITSQVIG NDATIAFAAS 350
    QGNFELNVFK PVIIYNFLQS TTLLTDGLRT FHDKCLIGLE ANETIIKKHL 400
    NESLMLVTAL NPHIGYENAA KIAKKAHAEG LTLKEAAMQS GLLTEEEFEK 450
    MVDPAKMVHP QG 462
    Length:462
    Mass (Da):50,785
    Last modified:October 1, 2000 - v1
    Checksum:i72601B22909B4899
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000004 Genomic DNA. Translation: BAB05164.1.
    PIRiE83830.
    RefSeqiNP_242311.1. NC_002570.2.
    WP_010897610.1. NC_002570.2.

    Genome annotation databases

    EnsemblBacteriaiBAB05164; BAB05164; BAB05164.
    GeneIDi890532.
    KEGGibha:BH1445.
    PATRICi18939985. VBIBacHal18977_1506.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000004 Genomic DNA. Translation: BAB05164.1 .
    PIRi E83830.
    RefSeqi NP_242311.1. NC_002570.2.
    WP_010897610.1. NC_002570.2.

    3D structure databases

    ProteinModelPortali Q9KCX4.
    SMRi Q9KCX4. Positions 4-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272558.BH1445.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB05164 ; BAB05164 ; BAB05164 .
    GeneIDi 890532.
    KEGGi bha:BH1445.
    PATRICi 18939985. VBIBacHal18977_1506.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    KOi K01679.
    OMAi AARHMKL.
    OrthoDBi EOG6V1M4M.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci BHAL272558:GJC5-1528-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. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
      Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
      Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

    Entry informationi

    Entry nameiFUMC_BACHD
    AccessioniPrimary (citable) accession number: Q9KCX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 85 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, 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