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Q8KTE1

- FUMC_METEA

UniProt

Q8KTE1 - FUMC_METEA

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      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 sitei195 – 1951Proton donor/acceptorBy similarity
    Active sitei325 – 3251By similarity
    Binding sitei326 – 3261SubstrateUniRule annotation
    Sitei338 – 3381Important 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

    BioCyciMEXT272630:GBY6-2704-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
    Synonyms:fumA
    Ordered Locus Names:MexAM1_META1p2857
    OrganismiMethylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1)
    Taxonomic identifieri272630 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium
    ProteomesiUP000009081: 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 – 472472Fumarate hydratase class IIPRO_0000161287Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ8KTE1.
    SMRiQ8KTE1. Positions 12-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni105 – 1073Substrate bindingUniRule annotation
    Regioni136 – 1394B siteUniRule annotation
    Regioni146 – 1483Substrate bindingUniRule annotation
    Regioni194 – 1952Substrate bindingUniRule annotation
    Regioni331 – 3333Substrate 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.

    Q8KTE1-1 [UniParc]FASTAAdd to Basket

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    MSPHENPSVE TRTESDTFGP IEVPAHRYWG AQTQRSIQNF KIGTERQPAP    50
    LVHALGIVKQ AAALVNKDLG GLDPKIADAI AESAAEVVAG KHDDEFPLVV 100
    WQTGSGTQSN MNANEVIASL ANERLGGKRG GKSPVHPNDH CNRGQSSNDT 150
    FPTAMHIAVA REVQERLLPA LSHLHTALDA KAKEFESIVK IGRTHLQDAT 200
    PVSLGQEFSG YAAQVALGGA RIAATLPGVL ALAQGGTAVG TGLNAHPEFA 250
    ERFAAKVAEL TGLPFTSAEN KFEALATHDA LVFLQGALTA LASGLFKIAN 300
    DIRLLGSGPR SGLGELSLPE NEPGSSIMPG KVNPTQCEAL TMVCAQVVGN 350
    GTTVSFAGSQ GHFELNVFKP VIANAVLQSV RILADASVSF TDNCVVGIKA 400
    NTDRISDLMS RSLMLVTALA PSIGYDKAAE IAKTAHKNGT TLKEEALRLG 450
    YVTDEEFERV VRPETMLAPS AE 472
    Length:472
    Mass (Da):49,739
    Last modified:October 1, 2002 - v1
    Checksum:i6B24EDD6A27775E7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF497854 Genomic DNA. Translation: AAN03819.1.
    CP001510 Genomic DNA. Translation: ACS40610.1.
    RefSeqiWP_003597776.1. NC_012808.1.
    YP_002963887.1. NC_012808.1.

    Genome annotation databases

    EnsemblBacteriaiACS40610; ACS40610; MexAM1_META1p2857.
    GeneIDi7992744.
    KEGGimea:Mex_1p2857.
    PATRICi22511447. VBIMetExt101010_2790.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF497854 Genomic DNA. Translation: AAN03819.1 .
    CP001510 Genomic DNA. Translation: ACS40610.1 .
    RefSeqi WP_003597776.1. NC_012808.1.
    YP_002963887.1. NC_012808.1.

    3D structure databases

    ProteinModelPortali Q8KTE1.
    SMRi Q8KTE1. Positions 12-469.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACS40610 ; ACS40610 ; MexAM1_META1p2857 .
    GeneIDi 7992744.
    KEGGi mea:Mex_1p2857.
    PATRICi 22511447. VBIMetExt101010_2790.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci MEXT272630:GBY6-2704-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. "Reconstruction of C3 and C4 metabolism in Methylobacterium extorquens AM1 using transposon mutagenesis."
      Van Dien S.J., Okubo Y., Hough M.T., Taitano T., Lidstrom M.E.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 14718 / DSM 1338 / AM1.

    Entry informationi

    Entry nameiFUMC_METEA
    AccessioniPrimary (citable) accession number: Q8KTE1
    Secondary accession number(s): C5AUK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 68 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