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Q8FX90

- FUMC_BRUSU

UniProt

Q8FX90 - FUMC_BRUSU

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Brucella suis biovar 1 (strain 1330)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 Mar 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 sitei188 – 1881Proton donor/acceptorBy similarity
    Active sitei318 – 3181By similarity
    Binding sitei319 – 3191SubstrateUniRule annotation
    Sitei331 – 3311Important 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 IIUniRule annotation (EC:4.2.1.2UniRule annotation)
    Short name:
    Fumarase CUniRule annotation
    Gene namesi
    Name:fumCUniRule annotation
    Ordered Locus Names:BRA0192, BS1330_II0189
    OrganismiBrucella suis biovar 1 (strain 1330)
    Taxonomic identifieri204722 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
    ProteomesiUP000000824: Chromosome II, UP000007104: Chromosome II

    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_0000161262Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi204722.BRA0192.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8FX90.
    SMRiQ8FX90. Positions 5-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni98 – 1003Substrate bindingUniRule annotation
    Regioni129 – 1324B siteUniRule annotation
    Regioni139 – 1413Substrate bindingUniRule annotation
    Regioni187 – 1882Substrate bindingUniRule annotation
    Regioni324 – 3263Substrate 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.

    Q8FX90-1 [UniParc]FASTAAdd to Basket

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    MAATRTETDT FGPIDVPADR YWGAQTQRSL QNFRIGGERM PLPLVHALGV    50
    VKRAAAETNI ALGKLDPVLG QVIAVAASEV IEGKLDDHFP LVVWQTGSGT 100
    QSNMNANEVI SNRAIELLGG EMGSKKPIHP NDHVNMSQSS NDSFPTAIHI 150
    ATAVETVNRL YPALEHLTKA LKVKEEAFKD IIKIGRTHTQ DATPVTLGQE 200
    FSGYRAALEY ARHRLEQSLA DVFLLAQGGT AVGTGLNAPV GFDKGFAEAV 250
    SEITGLSFKT APNKFEALAS HGAVLNFHGS LNALAADLFK IANDIRFLGS 300
    GPRSGLGELS LPENEPGSSI MPGKVNPTQA EAMTMVATQV FGNQTAVTVA 350
    ASQGHFELNV FKPVIAYNVL QSIRLLSDTM VSFADHCVEG IEPNTARIKE 400
    LLERSLMLVT ALAPAIGYDN AARIAKTAHK NGTTLREEAL ASGLVSEEDY 450
    DRLVRAERMI APQ 463
    Length:463
    Mass (Da):49,624
    Last modified:March 1, 2003 - v1
    Checksum:iC2F6DD271F19B4F8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014292 Genomic DNA. Translation: AAN33398.1.
    CP002998 Genomic DNA. Translation: AEM19675.1.
    RefSeqiNP_699393.1. NC_004311.2.
    YP_005613901.1. NC_017250.1.

    Genome annotation databases

    EnsemblBacteriaiAAN33398; AAN33398; BRA0192.
    AEM19675; AEM19675; BS1330_II0189.
    GeneIDi1164629.
    12139623.
    KEGGibms:BRA0192.
    bsi:BS1330_II0189.
    PATRICi17793181. VBIBruSui107850_2409.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014292 Genomic DNA. Translation: AAN33398.1 .
    CP002998 Genomic DNA. Translation: AEM19675.1 .
    RefSeqi NP_699393.1. NC_004311.2.
    YP_005613901.1. NC_017250.1.

    3D structure databases

    ProteinModelPortali Q8FX90.
    SMRi Q8FX90. Positions 5-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 204722.BRA0192.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN33398 ; AAN33398 ; BRA0192 .
    AEM19675 ; AEM19675 ; BS1330_II0189 .
    GeneIDi 1164629.
    12139623.
    KEGGi bms:BRA0192.
    bsi:BS1330_II0189.
    PATRICi 17793181. VBIBruSui107850_2409.

    Phylogenomic databases

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

    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: 1330.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1330.

    Entry informationi

    Entry nameiFUMC_BRUSU
    AccessioniPrimary (citable) accession number: Q8FX90
    Secondary accession number(s): G0KF31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 80 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. Brucella suis
      Brucella suis (strain 1330): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3