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Q885V0

- FUMC_PSESM

UniProt

Q885V0 - FUMC_PSESM

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Pseudomonas syringae pv. tomato (strain DC3000)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Jun 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 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

    BioCyciPSYR223283:GJIX-1762-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
    Synonyms:fumC-1
    Ordered Locus Names:PSPTO_1731
    OrganismiPseudomonas syringae pv. tomato (strain DC3000)
    Taxonomic identifieri223283 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002515: 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 – 464464Fumarate hydratase class IIPRO_0000161302Add
    BLAST

    2D gel databases

    World-2DPAGE0008:Q885V0.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi223283.PSPTO_1731.

    Structurei

    3D structure databases

    ProteinModelPortaliQ885V0.
    SMRiQ885V0. 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.
    PhylomeDBiQ885V0.

    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.

    Q885V0-1 [UniParc]FASTAAdd to Basket

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    MSRTETDSIG PIEVPEDAYW GAQTQRSLIN FAIGDQRMPL AVLHALTLIK    50
    KAAARVNDRN GDLPADIARL IEQAADEVLD GQHDAQFPLV VWQTGSGTQS 100
    NMNVNEVIAG RANELAGQGR GGKSPVHPND HVNRSQSSND CFPTAMHIAT 150
    AQAVKEQLLP AIAELSSGLA EQAARHMKLV KTGRTHMMDA TPITFGQELS 200
    GFVAQLDYAE KAIRAALPAV YELAQGGTAV GTGLNAPKGF AEAIAAELAA 250
    LSGLPFVTAP NKFAALAGHE PLAALSGALK TLAGTLMKIA NDLRLLGSGP 300
    RAGLAEVRLP ANEPGSSIMP GKVNPTQCEA LSMLACQVMG NDVTIGFAAS 350
    QGHLQLNVYK PVIIHNVLQS IRLLADGCSN FNEHCVAGME PDAEKMAEHL 400
    ERGLMLVTAL NPHIGYDKSA HIAKKAYTEG LTLREAALAL GYLTDEEFDA 450
    WVRPDKMLEA GSNG 464
    Length:464
    Mass (Da):49,077
    Last modified:June 1, 2003 - v1
    Checksum:i6B12FFF27257FFD2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016853 Genomic DNA. Translation: AAO55251.1.
    RefSeqiNP_791556.1. NC_004578.1.

    Genome annotation databases

    EnsemblBacteriaiAAO55251; AAO55251; PSPTO_1731.
    GeneIDi1183368.
    KEGGipst:PSPTO_1731.
    PATRICi19994714. VBIPseSyr93040_1758.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016853 Genomic DNA. Translation: AAO55251.1 .
    RefSeqi NP_791556.1. NC_004578.1.

    3D structure databases

    ProteinModelPortali Q885V0.
    SMRi Q885V0. Positions 3-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 223283.PSPTO_1731.

    2D gel databases

    World-2DPAGE 0008:Q885V0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO55251 ; AAO55251 ; PSPTO_1731 .
    GeneIDi 1183368.
    KEGGi pst:PSPTO_1731.
    PATRICi 19994714. VBIPseSyr93040_1758.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    KOi K01679.
    OMAi AARHMKL.
    OrthoDBi EOG6V1M4M.
    PhylomeDBi Q885V0.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci PSYR223283:GJIX-1762-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: DC3000.

    Entry informationi

    Entry nameiFUMC_PSESM
    AccessioniPrimary (citable) accession number: Q885V0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 82 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