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Q8YB50

- FUMC_BRUME

UniProt

Q8YB50 - FUMC_BRUME

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (15 Dec 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:BMEII1051
    OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
    Taxonomic identifieri224914 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
    ProteomesiUP000000419: 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_0000161261Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    IntActiQ8YB50. 1 interaction.
    STRINGi224914.BMEII1051.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8YB50.
    SMRiQ8YB50. 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

    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.

    Q8YB50-1 [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:December 15, 2003 - v2
    Checksum:iC2F6DD271F19B4F8
    GO

    Sequence cautioni

    The sequence AAL54293.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008918 Genomic DNA. Translation: AAL54293.1. Different initiation.
    PIRiAB3641.
    RefSeqiNP_542029.2. NC_003318.1.

    Genome annotation databases

    EnsemblBacteriaiAAL54293; AAL54293; BMEII1051.
    GeneIDi1198823.
    KEGGibme:BMEII1051.
    PATRICi17856895. VBIBruMel92729_3406.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE008918 Genomic DNA. Translation: AAL54293.1 . Different initiation.
    PIRi AB3641.
    RefSeqi NP_542029.2. NC_003318.1.

    3D structure databases

    ProteinModelPortali Q8YB50.
    SMRi Q8YB50. Positions 5-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8YB50. 1 interaction.
    STRINGi 224914.BMEII1051.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL54293 ; AAL54293 ; BMEII1051 .
    GeneIDi 1198823.
    KEGGi bme:BMEII1051.
    PATRICi 17856895. VBIBruMel92729_3406.

    Phylogenomic databases

    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: 16M / ATCC 23456 / NCTC 10094.

    Entry informationi

    Entry nameiFUMC_BRUME
    AccessioniPrimary (citable) accession number: Q8YB50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 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 melitensis
      Brucella melitensis (strain 16M): 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