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Q9I587

- FUMC2_PSEAE

UniProt

Q9I587 - FUMC2_PSEAE

Protein

Fumarate hydratase class II 2

Gene

fumC2

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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

    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase class II 2UniRule annotation (EC:4.2.1.2UniRule annotation)
    Short name:
    Fumarase C 2UniRule annotation
    Gene namesi
    Name:fumC2UniRule annotation
    Ordered Locus Names:PA0854
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA0854.

    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 II 2PRO_0000161300Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi208964.PA0854.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9I587.
    SMRiQ9I587. Positions 3-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni96 – 983Substrate 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.
    PhylomeDBiQ9I587.

    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.

    Q9I587-1 [UniParc]FASTAAdd to Basket

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    MSRTETDSLG TIEVPDDAYW GAQTQRSLEN FAIGGQRMPL AVIHALALIK    50
    KAAARVNDHL GELPPEVARL IEQAADEVLA GRHDEHFPLV VWQTGSGTQT 100
    NMNVNEVIAG RANELAGNPR GGKSPVHPND HVNRAQSSND SFPTAMHIAA 150
    AKAVHEQLLP AIAELSGGLA EQSARHASLV KTGRTHLMDA TPITFGQELS 200
    AFVAQLDYAE RAIRAALPAV YQLAQGGTAV GTGLNAPKGF ADAIAAEIAA 250
    ESGLPFVAAP NKFAALAGHE PLVILSGALK SLAVALMKIA NDLRLLGSGP 300
    RAGFAEVKLP ANEPGSSIMP GKVNPTQCEA LSMLACQVMG NDSTISFAAS 350
    QGHLQLNVFK PVIVYNLLES IRLLADGCRN FNKHCVAGLE PDAQRMADLL 400
    ERGLMLVTAL NPHIGYDKAA EIAKKAYAEG TTLRAAALQL GYLDEAQFDE 450
    WVRPEQMLEA GHHG 464
    Length:464
    Mass (Da):49,122
    Last modified:March 1, 2001 - v1
    Checksum:iB0520F835C0DDF61
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004091 Genomic DNA. Translation: AAG04243.1.
    PIRiH83538.
    RefSeqiNP_249545.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG04243; AAG04243; PA0854.
    GeneIDi878044.
    KEGGipae:PA0854.
    PATRICi19835988. VBIPseAer58763_0886.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004091 Genomic DNA. Translation: AAG04243.1 .
    PIRi H83538.
    RefSeqi NP_249545.1. NC_002516.2.

    3D structure databases

    ProteinModelPortali Q9I587.
    SMRi Q9I587. Positions 3-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA0854.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG04243 ; AAG04243 ; PA0854 .
    GeneIDi 878044.
    KEGGi pae:PA0854.
    PATRICi 19835988. VBIPseAer58763_0886.

    Organism-specific databases

    PseudoCAPi PA0854.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    KOi K01679.
    OMAi AARHMKL.
    OrthoDBi EOG6V1M4M.
    PhylomeDBi Q9I587.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .

    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: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

    Entry informationi

    Entry nameiFUMC2_PSEAE
    AccessioniPrimary (citable) accession number: Q9I587
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 86 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