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Q82ID7

- FUMC_STRAW

UniProt

Q82ID7 - FUMC_STRAW

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 78 (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 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

    BioCyciSAVE227882:GJU1-3245-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:SAV_3221
    OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
    Taxonomic identifieri227882 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
    ProteomesiUP000000428: 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 – 467467Fumarate hydratase class IIPRO_0000161321Add
    BLAST

    Proteomic databases

    PRIDEiQ82ID7.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi227882.SAV_3221.

    Structurei

    3D structure databases

    ProteinModelPortaliQ82ID7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni104 – 1063Substrate 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.
    HOGENOMiHOG000061737.
    KOiK01679.
    OMAiHANQMAS.
    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.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q82ID7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDEDDKQNY RVEHDSMGEV RVPADAKWRA QTQRAVENFP ISGQRLERAH    50
    IEALARIKGA AAKVNAELGV LDKDVAEAIQ EAAAEVAEGR WDEHFPVDVF 100
    QTGSGTSSNM NANEVIATLA TERLGRDVHP NDHVNASQSS NDVFPSSIHI 150
    AATAAVTRDL VPALEHLAAA LGRKSEEFAD VVKAGRTHLM DATPVTLGQE 200
    FGGYAAQVRY GVERLAASLP RLAELPLGGT AVGTGINTPP GFSAAVIAEV 250
    ARVTGLPLTE ARDHFEAQGA RDGIVETSGQ LRTIAVGLTK IANDLRWMAS 300
    GPRTGLSEIS LPDLQPGSSI MPGKVNPVIP EAVLMVAAQV TGNDATVAAA 350
    GAAGNFELNV MLPVIAKNVL ESVRLLAHVS RLLADRTVDG IVAHRDRARE 400
    YAESSPSVVT PLNKYIGYEE AAKVAKKALA ERQTIRQVVL ESGYVDRGDL 450
    TLEQLDEALD VLRMTHP 467
    Length:467
    Mass (Da):49,801
    Last modified:June 1, 2003 - v1
    Checksum:i5D984D1060B87F36
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000030 Genomic DNA. Translation: BAC70932.1.
    RefSeqiNP_824397.1. NC_003155.4.
    WP_010984651.1. NC_003155.4.

    Genome annotation databases

    EnsemblBacteriaiBAC70932; BAC70932; SAV_3221.
    GeneIDi1210693.
    KEGGisma:SAV_3221.
    PATRICi23720069. VBIStrAve112782_3441.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000030 Genomic DNA. Translation: BAC70932.1 .
    RefSeqi NP_824397.1. NC_003155.4.
    WP_010984651.1. NC_003155.4.

    3D structure databases

    ProteinModelPortali Q82ID7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 227882.SAV_3221.

    Proteomic databases

    PRIDEi Q82ID7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC70932 ; BAC70932 ; SAV_3221 .
    GeneIDi 1210693.
    KEGGi sma:SAV_3221.
    PATRICi 23720069. VBIStrAve112782_3441.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061737.
    KOi K01679.
    OMAi HANQMAS.
    OrthoDBi EOG6V1M4M.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci SAVE227882:GJU1-3245-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.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
      Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
      Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
    2. "Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
      Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
      Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

    Entry informationi

    Entry nameiFUMC_STRAW
    AccessioniPrimary (citable) accession number: Q82ID7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 78 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