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Q9ZJQ9

- FUMC_HELPJ

UniProt

Q9ZJQ9 - FUMC_HELPJ

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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

    BioCyciHPYL85963:GJB9-1281-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:jhp_1245
    OrganismiHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
    Taxonomic identifieri85963 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
    ProteomesiUP000000804: 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_0000161281Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi85963.jhp1245.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZJQ9.
    SMRiQ9ZJQ9. 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

    eggNOGiCOG0114.
    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.

    Q9ZJQ9-1 [UniParc]FASTAAdd to Basket

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    MQFRIEHDTM GEIKVDDSQY WGAQTQRSLE NFKIGTEKMP KELIGAFAKL    50
    KRSLAVVNHK LGKLSLEKSQ AIIKACDCIL KGELCGEFPL AIWQTGSGTQ 100
    TNMNLNEVIA NKATEILGGN FREKKLIHPN DDVNMSQSSN DTFPTAMHVV 150
    SVLEITHKLL PSLENLLKTF KEKSQQFKEI VKIGRTHLQD ATPLTLGQEF 200
    SGYASMLEHS KQQILESLEH LRELAIGGTA VGTGLNAHKE LSEKVAEELS 250
    QFSGVKFISA PNKFHALTSH DAIAYAHGAF KALAANLMKI ANDIRWLASG 300
    PRCGLGELNI PENEPGSSIM PGKVNPTQCE AMTMVAVQVM GNDTAIGIAA 350
    SQGNFELNVF KPVIIYNFLQ SLRLLSDSME SFNIHCASGI EPNKEKIDYY 400
    LHHSLMLVTA LNPHVGYENA AKIAKNAHKK GISLKESALE LKLLSAEDFD 450
    QFVVPEKMIG PKA 463
    Length:463
    Mass (Da):50,920
    Last modified:May 1, 1999 - v1
    Checksum:iEF8EEF9CABD1D485
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001439 Genomic DNA. Translation: AAD06830.1.
    PIRiH71830.
    RefSeqiNP_223963.1. NC_000921.1.

    Genome annotation databases

    EnsemblBacteriaiAAD06830; AAD06830; jhp_1245.
    GeneIDi890413.
    KEGGihpj:jhp1245.
    PATRICi20607334. VBIHelPyl98156_1348.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE001439 Genomic DNA. Translation: AAD06830.1 .
    PIRi H71830.
    RefSeqi NP_223963.1. NC_000921.1.

    3D structure databases

    ProteinModelPortali Q9ZJQ9.
    SMRi Q9ZJQ9. Positions 4-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 85963.jhp1245.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAD06830 ; AAD06830 ; jhp_1245 .
    GeneIDi 890413.
    KEGGi hpj:jhp1245.
    PATRICi 20607334. VBIHelPyl98156_1348.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci HPYL85963:GJB9-1281-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: J99 / ATCC 700824.

    Entry informationi

    Entry nameiFUMC_HELPJ
    AccessioniPrimary (citable) accession number: Q9ZJQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 99 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