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Q8TS07

- FUMC_METAC

UniProt

Q8TS07 - FUMC_METAC

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
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 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 sitei200 – 2001Proton donor/acceptorBy similarity
    Active sitei330 – 3301By similarity
    Binding sitei331 – 3311SubstrateUniRule annotation
    Sitei343 – 3431Important 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

    BioCyciMACE188937:GI2O-1012-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:MA_1001
    OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
    Taxonomic identifieri188937 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
    ProteomesiUP000002487: 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 – 484484Fumarate hydratase class IIPRO_0000161333Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi188937.MA1001.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TS07.
    SMRiQ8TS07. Positions 16-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni110 – 1123Substrate bindingUniRule annotation
    Regioni141 – 1444B siteUniRule annotation
    Regioni151 – 1533Substrate bindingUniRule annotation
    Regioni199 – 2002Substrate bindingUniRule annotation
    Regioni336 – 3383Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0114.
    KOiK01679.
    OMAiMFSGPMT.
    PhylomeDBiQ8TS07.

    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.

    Q8TS07-1 [UniParc]FASTAAdd to Basket

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    MPSILDLPIG TGATGKRKES DSLGEVEVPA DHYWGAQTQR SLIHFSIGDD    50
    YMPKEVYHAY GYVKKAAALV NEAAGIIPPW KAELIARVAD EVIAGKLDSE 100
    FPLYVWQTGS GTQSNMNVNE VISNRAIQLV GGSLGSKHPV HPNDDVNMSQ 150
    SSNDTFPTAM HIATVLEFSN RLIPAVTVLE ESIWAKAREW VDIVKIGRTH 200
    LQDATPLTVG QEWSGYATQL DDALAFVKHS LRGLYRLAIG GTAVGTGINT 250
    PPDFGEKVAD EIARLTGHPF VTAPNKFAAQ GSLDAMVTSS AALRTLAVAL 300
    MKIANDLQWL GSGPRSGLHE LILPSDEPGS SIMPGKVNPT QEEAMLMVCI 350
    QVIGEDNAVA FAGSQGNFEL NAMCPIIINN VLHSARTLGD ACVKFREYGI 400
    NGIMLDRSRI DKFVGTSLML VTALSPVIGY DKASAIVQRA LDENTTLREA 450
    AVKGGFISAE DFDRIVDPKK MVGDPRHDLK LASE 484
    Length:484
    Mass (Da):52,127
    Last modified:December 15, 2003 - v2
    Checksum:i06F0EFE5664BEEC8
    GO

    Sequence cautioni

    The sequence AAM04432.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010299 Genomic DNA. Translation: AAM04432.1. Different initiation.
    RefSeqiNP_615952.1. NC_003552.1.

    Genome annotation databases

    EnsemblBacteriaiAAM04432; AAM04432; MA_1001.
    GeneIDi1472891.
    KEGGimac:MA1001.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010299 Genomic DNA. Translation: AAM04432.1 . Different initiation.
    RefSeqi NP_615952.1. NC_003552.1.

    3D structure databases

    ProteinModelPortali Q8TS07.
    SMRi Q8TS07. Positions 16-473.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 188937.MA1001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM04432 ; AAM04432 ; MA_1001 .
    GeneIDi 1472891.
    KEGGi mac:MA1001.

    Phylogenomic databases

    eggNOGi COG0114.
    KOi K01679.
    OMAi MFSGPMT.
    PhylomeDBi Q8TS07.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci MACE188937:GI2O-1012-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 of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity."
      Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.
      , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.
      Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

    Entry informationi

    Entry nameiFUMC_METAC
    AccessioniPrimary (citable) accession number: Q8TS07
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 80 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, 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