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Q7NZ02

- FUMC_CHRVO

UniProt

Q7NZ02 - FUMC_CHRVO

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (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 sitei189 – 1891Proton donor/acceptorBy similarity
    Active sitei319 – 3191By similarity
    Binding sitei320 – 3201SubstrateUniRule annotation
    Sitei332 – 3321Important 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

    BioCyciCVIO243365:GHUD-1149-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:CV_1120
    OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
    Taxonomic identifieri243365 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
    ProteomesiUP000001424: 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 – 461461Fumarate hydratase class IIPRO_0000161270Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi243365.CV_1120.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7NZ02.
    SMRiQ7NZ02. Positions 5-461.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni99 – 1013Substrate bindingUniRule annotation
    Regioni130 – 1334B siteUniRule annotation
    Regioni140 – 1423Substrate bindingUniRule annotation
    Regioni188 – 1892Substrate bindingUniRule annotation
    Regioni325 – 3273Substrate 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.

    Q7NZ02-1 [UniParc]FASTAAdd to Basket

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    MTKTVRSETD TFGPIDVPAA ALWGAQTQRS LAHFRISSEK MPPELILALA    50
    RVKRACAEAN RGLGKLDDAK AAAIAGAADE VLAGRHDGEF PLSVWQTGSG 100
    TQSNMNMNEV LANRASELLG GRRGPGRLVH PNDDVNLGQS SNDIFPTAMH 150
    VAAATQVKER LLPSLDLLRH ALESKAEAFA DVVKIGRTHL QDATPLTLGQ 200
    EISGWAAQLA LSEQAVRAAL PMLCQLAVGG TAVGTGLNTD PSFGAAVAAR 250
    LAEQSGLPFE SAGNKFAALA GHEPLVFAHG ALKTLAAALM KIANDIRWLA 300
    SGPRSGLGEL SLPENEPGSS IMPGKVNPTQ CEAMTMLCCQ VLGNDAALAI 350
    GAASGNFELN VFKPLIAHNF LQSARLLADG MDSLREHCVD GMEANRARIA 400
    ELMARSLMLV TALNPHIGYD KAAAIAKHAH RHGTTLREAA LALGHLSAEQ 450
    FDAWVRPEDM V 461
    Length:461
    Mass (Da):48,610
    Last modified:December 15, 2003 - v1
    Checksum:i49B09E5DD6B0B90F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016825 Genomic DNA. Translation: AAQ58795.1.
    RefSeqiNP_900790.1. NC_005085.1.

    Genome annotation databases

    EnsemblBacteriaiAAQ58795; AAQ58795; CV_1120.
    GeneIDi2550480.
    KEGGicvi:CV_1120.
    PATRICi21437054. VBIChrVio67196_1109.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016825 Genomic DNA. Translation: AAQ58795.1 .
    RefSeqi NP_900790.1. NC_005085.1.

    3D structure databases

    ProteinModelPortali Q7NZ02.
    SMRi Q7NZ02. Positions 5-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243365.CV_1120.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAQ58795 ; AAQ58795 ; CV_1120 .
    GeneIDi 2550480.
    KEGGi cvi:CV_1120.
    PATRICi 21437054. VBIChrVio67196_1109.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci CVIO243365:GHUD-1149-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. "The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
      Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A.
      , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
      Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

    Entry informationi

    Entry nameiFUMC_CHRVO
    AccessioniPrimary (citable) accession number: Q7NZ02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 80 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