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Q7VR50

- FUMC_BLOFL

UniProt

Q7VR50 - FUMC_BLOFL

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Blochmannia floridanus
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    • Comment

    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 sitei172 – 1721Proton donor/acceptorBy similarity
    Active sitei302 – 3021By similarity
    Binding sitei303 – 3031SubstrateUniRule annotation
    Sitei315 – 3151Important 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

    BioCyciBFLO203907:GHF7-373-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:Bfl373
    OrganismiBlochmannia floridanus
    Taxonomic identifieri203907 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeant endosymbiontsCandidatus Blochmannia
    ProteomesiUP000002192: 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 – 448448Fumarate hydratase class IIPRO_0000161264Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi203907.Bfl373.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7VR50.
    SMRiQ7VR50. Positions 4-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni83 – 853Substrate bindingUniRule annotation
    Regioni113 – 1164B siteUniRule annotation
    Regioni123 – 1253Substrate bindingUniRule annotation
    Regioni171 – 1722Substrate bindingUniRule annotation
    Regioni308 – 3103Substrate 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.

    Q7VR50-1 [UniParc]FASTAAdd to Basket

    « Hide

    MICNRLWGDQ TESSLKFFNI STEKMPWELI KALAQIKRVS AQVNYDLKLL    50
    DYERSQAIIA AVDEILSGNH KNEFPLSVWQ TGSGTQSNMN MNEVLANRAN 100
    ELLRKNQINI VVHPNDHVNK SQSSNDVFPS AMHIAAVVNL KTKLIPVIKL 150
    LQKTFLKKSI EFRNIIKIGR THLQDAIPLT LGQEISGWDF MLKNNTNHIQ 200
    STILDLSALA LGGTAVGTGF SAHVEYAERV VLGLSKLIHH SFFSAPNKFE 250
    SLSTCDAIVY SHGTLKGLAI SMMKIANDIR LLSSGPQCGL GELIIPANEP 300
    GSSIMPGKVN PTQCESMTMS CCQVMGNDLS ISLGGSSGQL QLNTYRPLII 350
    YNFLQSIRLL TDSIKNFHDY CIVGIRPKFK RIEKLLNKSL MLVTALSSHI 400
    GYDKSAQIAQ TAYLNGITLK AASIQSGYVT EKQFDDWVCP ENMIYPDM 448
    Length:448
    Mass (Da):49,649
    Last modified:October 1, 2003 - v1
    Checksum:iCDEC7863B7D10F2D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248583 Genomic DNA. Translation: CAD83439.1.
    RefSeqiNP_878664.1. NC_005061.1.
    WP_011126647.1. NC_005061.1.

    Genome annotation databases

    EnsemblBacteriaiCAD83439; CAD83439; Bfl373.
    GeneIDi1499573.
    KEGGibfl:Bfl373.
    PATRICi31964347. VBICanBlo38691_0363.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248583 Genomic DNA. Translation: CAD83439.1 .
    RefSeqi NP_878664.1. NC_005061.1.
    WP_011126647.1. NC_005061.1.

    3D structure databases

    ProteinModelPortali Q7VR50.
    SMRi Q7VR50. Positions 4-444.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 203907.Bfl373.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD83439 ; CAD83439 ; Bfl373 .
    GeneIDi 1499573.
    KEGGi bfl:Bfl373.
    PATRICi 31964347. VBICanBlo38691_0363.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci BFLO203907:GHF7-373-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].

    Entry informationi

    Entry nameiFUMC_BLOFL
    AccessioniPrimary (citable) accession number: Q7VR50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 76 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