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Q81SA0

- FUMC_BACAN

UniProt

Q81SA0 - FUMC_BACAN

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Bacillus anthracis
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 86 (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 sitei186 – 1861Proton donor/acceptorBy similarity
    Active sitei316 – 3161By similarity
    Binding sitei317 – 3171SubstrateUniRule annotation
    Sitei329 – 3291Important 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

    BioCyciANTHRA:FUMC-MONOMER.
    BANT260799:GJAJ-1708-MONOMER.
    BANT261594:GJ7F-1779-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:BA_1767, GBAA_1767, BAS1637
    OrganismiBacillus anthracis
    Taxonomic identifieri1392 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000000427: Chromosome, UP000000594: Chromosome, UP000005639: 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 – 462462Fumarate hydratase class IIPRO_0000161252Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi198094.BA_1767.

    Structurei

    3D structure databases

    ProteinModelPortaliQ81SA0.
    SMRiQ81SA0. Positions 4-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 993Substrate bindingUniRule annotation
    Regioni127 – 1304B siteUniRule annotation
    Regioni137 – 1393Substrate bindingUniRule annotation
    Regioni185 – 1862Substrate bindingUniRule annotation
    Regioni322 – 3243Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    KOiK01679.
    OMAiIAFNDNC.
    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.

    Q81SA0-1 [UniParc]FASTAAdd to Basket

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    MEYRIERDTL GEIKVPADKL WAAQTQRSKE NFPIGTEQMP LEIVKAFAIL    50
    KKSAALSNQK LGKLSEEKAE AIVVAADEII AGKWNEHFPL VVWQTGSGTQ 100
    SNMNVNEVIA NRGNQILKEK GSDVHIHPND DVNMSQSSND TFPTALHVAC 150
    VLAVENHVLP AITKLKETLA EKVTAFEHII KIGRTHLQDA TPLTLGQEIS 200
    GWHRMLEKTE RMIAESNTYM KELAIGGTAV GTGINAHPKF GEMVSEEISQ 250
    FTGKQFISAP NKFHALTSHD EVVYTHGALK ALAADLMKIA NDVRWLASGP 300
    RSGLGEIIIP ANEPGSSIMP GKVNPTQSEA LTMVVAQVMG NDATIGFAAS 350
    QGNFELNVFK PVIAYNFLQS AHLLADAIVS FNDNCAVGIE ADEEIIKENV 400
    NRSLMLVTAL NPHIGYENAA KIAKHAHKEG LTLKEAALQS GLLTEEQFNE 450
    IVDPKKMIAP KE 462
    Length:462
    Mass (Da):50,345
    Last modified:June 1, 2003 - v1
    Checksum:i0FB897C31FAC981D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016879 Genomic DNA. Translation: AAP25681.1.
    AE017334 Genomic DNA. Translation: AAT30883.1.
    AE017225 Genomic DNA. Translation: AAT53954.1.
    RefSeqiNP_844195.1. NC_003997.3.
    YP_018408.1. NC_007530.2.
    YP_027903.1. NC_005945.1.

    Genome annotation databases

    EnsemblBacteriaiAAP25681; AAP25681; BA_1767.
    AAT30883; AAT30883; GBAA_1767.
    AAT53954; AAT53954; BAS1637.
    GeneIDi1086574.
    2818045.
    2851297.
    KEGGiban:BA_1767.
    bar:GBAA_1767.
    bat:BAS1637.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016879 Genomic DNA. Translation: AAP25681.1 .
    AE017334 Genomic DNA. Translation: AAT30883.1 .
    AE017225 Genomic DNA. Translation: AAT53954.1 .
    RefSeqi NP_844195.1. NC_003997.3.
    YP_018408.1. NC_007530.2.
    YP_027903.1. NC_005945.1.

    3D structure databases

    ProteinModelPortali Q81SA0.
    SMRi Q81SA0. Positions 4-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198094.BA_1767.

    Protocols and materials databases

    DNASUi 1086574.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP25681 ; AAP25681 ; BA_1767 .
    AAT30883 ; AAT30883 ; GBAA_1767 .
    AAT53954 ; AAT53954 ; BAS1637 .
    GeneIDi 1086574.
    2818045.
    2851297.
    KEGGi ban:BA_1767.
    bar:GBAA_1767.
    bat:BAS1637.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci ANTHRA:FUMC-MONOMER.
    BANT260799:GJAJ-1708-MONOMER.
    BANT261594:GJ7F-1779-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. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
      Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
      , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
      Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames / isolate Porton.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames ancestor.
    3. "Complete genome sequence of Bacillus anthracis Sterne."
      Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Sterne.

    Entry informationi

    Entry nameiFUMC_BACAN
    AccessioniPrimary (citable) accession number: Q81SA0
    Secondary accession number(s): Q6I0I3, Q6KUE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 86 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