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Q7WG65

- FUMC_BORBR

UniProt

Q7WG65 - FUMC_BORBR

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Oct 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 sitei187 – 1871Proton donor/acceptorBy similarity
    Active sitei317 – 3171By similarity
    Binding sitei318 – 3181SubstrateUniRule annotation
    Sitei330 – 3301Important 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

    BioCyciBBRO257310:BB4054-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:BB4054
    OrganismiBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
    Taxonomic identifieri257310 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
    ProteomesiUP000001027: 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_0000161256Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi257310.BB4054.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7WG65.
    SMRiQ7WG65. Positions 4-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 993Substrate bindingUniRule annotation
    Regioni128 – 1314B siteUniRule annotation
    Regioni138 – 1403Substrate bindingUniRule annotation
    Regioni186 – 1872Substrate bindingUniRule annotation
    Regioni323 – 3253Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    KOiK01679.
    OMAiMESFNIH.
    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.

    Q7WG65-1 [UniParc]FASTAAdd to Basket

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    MKTRTEKDTF GPIEVPEQHL WGAQTQRSLH FFAISTEKMP VPLVAAMARL    50
    KRAAAKVNAE LGELDPQVAD AIMRAADEVV AGKWPDEFPL SVWQTGSGTQ 100
    SNMNMNEVLA NRASELLGGE RGEGRKVHPN DHVNRGQSSN DTFPTAMHVA 150
    AAVEVEHRVL PALKALRGTL AAKSAAFYDI VKIGRTHLQD ATPLTLGQEI 200
    SGYVAQLDLA EQQIRATLAG LHQLAIGGTA VGTGLNAHPQ FSAKVSAELA 250
    HDTGSAFVSA PNKFQALASH EALLFAHGAL KTLAAGLMKI ANDVRWLASG 300
    PRSGLGEISI PENEPGSSIM PGKVNPTQCE AVTMLAAQVM GNDVAINVGG 350
    ASGNFELNVF KPLVIHNFLQ SVRLLADGMV SFDKHCAAGI EPNRERITEL 400
    VERSLMLVTA LNPHIGYDKA AQIAKKAHKE NLSLKEAALA LGHLTEAQFA 450
    EWVVPGDMTN ARR 463
    Length:463
    Mass (Da):49,491
    Last modified:October 1, 2003 - v1
    Checksum:i8D96DAFACB625AE1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX640449 Genomic DNA. Translation: CAE34417.1.
    RefSeqiNP_890588.1. NC_002927.3.

    Genome annotation databases

    EnsemblBacteriaiCAE34417; CAE34417; BB4054.
    GeneIDi2660076.
    KEGGibbr:BB4054.
    PATRICi21141531. VBIBorBro124907_4120.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX640449 Genomic DNA. Translation: CAE34417.1 .
    RefSeqi NP_890588.1. NC_002927.3.

    3D structure databases

    ProteinModelPortali Q7WG65.
    SMRi Q7WG65. Positions 4-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 257310.BB4054.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE34417 ; CAE34417 ; BB4054 .
    GeneIDi 2660076.
    KEGGi bbr:BB4054.
    PATRICi 21141531. VBIBorBro124907_4120.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci BBRO257310:BB4054-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. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
      Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
      , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
      Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-588 / NCTC 13252 / RB50.

    Entry informationi

    Entry nameiFUMC_BORBR
    AccessioniPrimary (citable) accession number: Q7WG65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 73 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