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Q72VY3

- FUMC_LEPIC

UniProt

Q72VY3 - FUMC_LEPIC

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
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 (05 Jul 2004)
      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

    BioCyciLINT267671:GHQI-161-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:LIC_10162
    OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
    Taxonomic identifieri267671 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
    ProteomesiUP000007037: Chromosome I

    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 – 464464Fumarate hydratase class IIPRO_0000161282Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi267671.LIC10162.

    Structurei

    3D structure databases

    ProteinModelPortaliQ72VY3.
    SMRiQ72VY3. Positions 4-459.
    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

    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.

    Q72VY3-1 [UniParc]FASTAAdd to Basket

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    MKTRIETDSM GEIAVDDSKY WGAQTERSLH HFHIGNDRFP REMIRALGIL    50
    KKSAAVVNAE LGLLSEDKKK LIVQAADEVI SGKLDEHFPL SVWQTGSGTQ 100
    TNMNSNEVIS NRAIEIAGGV KGSKKPIHPN DDVNKAQSSN DTFPTAMHIA 150
    AAEQLNQKLI PALIQLKETF KKKTDEFQNI IKIGRTHLQD ATPLTLGQEF 200
    SGYVQQLEYN IARVKAVLPS VYRLALGGTA VGTGLNTHPQ FAVKAAAQIA 250
    KETGLPFVSA ENKFEALAAH DSLVETSGVL KTIAASLMKI ANDIRWLSSG 300
    PRCGIGEISI PENEPGSSIM PGKVNPTQSE QMTMVAAQVI ANDVAVNIGG 350
    ASGNFELNVF KPLIIHNVLN SIRLLSDSCV SFEEHCARGI IPNKEKLNEH 400
    LNNSLMLVTA LNPHIGYDNA AKIAKNAHKK GTTLKESGIE LGLLTSEQFD 450
    QWVLPEKMIH PSVD 464
    Length:464
    Mass (Da):50,397
    Last modified:July 5, 2004 - v1
    Checksum:iAE316E36BAB02FA8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016823 Genomic DNA. Translation: AAS68791.1.
    RefSeqiYP_000154.1. NC_005823.1.

    Genome annotation databases

    EnsemblBacteriaiAAS68791; AAS68791; LIC_10162.
    GeneIDi2771729.
    KEGGilic:LIC10162.
    PATRICi22372002. VBILepInt6257_0178.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016823 Genomic DNA. Translation: AAS68791.1 .
    RefSeqi YP_000154.1. NC_005823.1.

    3D structure databases

    ProteinModelPortali Q72VY3.
    SMRi Q72VY3. Positions 4-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 267671.LIC10162.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS68791 ; AAS68791 ; LIC_10162 .
    GeneIDi 2771729.
    KEGGi lic:LIC10162.
    PATRICi 22372002. VBILepInt6257_0178.

    Phylogenomic databases

    KOi K01679.
    OMAi MESFNIH.
    OrthoDBi EOG6V1M4M.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci LINT267671:GHQI-161-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 genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis."
      Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S.
      , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.
      J. Bacteriol. 186:2164-2172(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Fiocruz L1-130.

    Entry informationi

    Entry nameiFUMC_LEPIC
    AccessioniPrimary (citable) accession number: Q72VY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: July 5, 2004
    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