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Q8XQE8

- FUMC_RALSO

UniProt

Q8XQE8 - FUMC_RALSO

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      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

    BioCyciRSOL267608:GCVU-4788-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:RSp1279
    ORF Names:RS05324
    Encoded oniPlasmid megaplasmid Rsp0 Publication
    OrganismiRalstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
    Taxonomic identifieri267608 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia
    ProteomesiUP000001436: Plasmid megaplasmid Rsp

    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_0000161303Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi267608.RSp1279.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8XQE8.
    SMRiQ8XQE8. 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.
    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.

    Q8XQE8-1 [UniParc]FASTAAdd to Basket

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    MTTRTERDTF GPIEVPADRL WGAQTQRSLQ NFDIAGDRMP RELIDALARI    50
    KRASAAVNQR LGLLPADKAN AVIAAADEVI AGKHPGEFPL VVWQTGSGTQ 100
    SNMNMNEVLA NRASELLGGE RGEARLVHPN DDVNRSQSSN DVFPTAMHVA 150
    AVTAITRHLL PSLRALRETL ARKAIDFDDI IKIGRTHLQD ATPLTLGQEF 200
    SGYAAQLQHS ETHLNAALPH LCELALGGTA VGTGLNAPAG YAEQVAAELA 250
    ALTGLPFVTS PNKFETMASA DGLVHAHGAL KTLAASLTKI ANDIRWLASG 300
    PRSGLGELSI PENEPGSSIM PGKVNPTQSE AMTMLCAQVF GNDVAVNIGG 350
    ASGNFELNVF RPMIAYNFLH SARLLADGMR SFNDHCAVGI EPNRERIAEL 400
    VQRSLMLVTA LNPHIGYDKS AQIAKKAHKE GTSLREAALA LGYVTAEQFD 450
    AWVRPEQMVG R 461
    Length:461
    Mass (Da):49,403
    Last modified:March 1, 2002 - v1
    Checksum:i8A44D62B53EDE18B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL646053 Genomic DNA. Translation: CAD18430.1.
    RefSeqiNP_522838.1. NC_003296.1.
    WP_011004561.1. NC_003296.1.

    Genome annotation databases

    EnsemblBacteriaiCAD18430; CAD18430; RSp1279.
    GeneIDi1223591.
    KEGGirso:RSp1279.
    PATRICi20268209. VBIRalSol70888_4772.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL646053 Genomic DNA. Translation: CAD18430.1 .
    RefSeqi NP_522838.1. NC_003296.1.
    WP_011004561.1. NC_003296.1.

    3D structure databases

    ProteinModelPortali Q8XQE8.
    SMRi Q8XQE8. Positions 4-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 267608.RSp1279.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD18430 ; CAD18430 ; RSp1279 .
    GeneIDi 1223591.
    KEGGi rso:RSp1279.
    PATRICi 20268209. VBIRalSol70888_4772.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci RSOL267608:GCVU-4788-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: GMI1000.

    Entry informationi

    Entry nameiFUMC_RALSO
    AccessioniPrimary (citable) accession number: Q8XQE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: March 1, 2002
    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, Plasmid, 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