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Q983U5

- FUMC_RHILO

UniProt

Q983U5 - FUMC_RHILO

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Rhizobium loti (strain MAFF303099) (Mesorhizobium loti)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Oct 2001)
      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 sitei190 – 1901Proton donor/acceptorBy similarity
    Active sitei320 – 3201By similarity
    Binding sitei321 – 3211SubstrateUniRule annotation
    Sitei333 – 3331Important 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

    BioCyciMLOT266835:GJ9L-6478-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:mll8172
    OrganismiRhizobium loti (strain MAFF303099) (Mesorhizobium loti)
    Taxonomic identifieri266835 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
    ProteomesiUP000000552: 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 – 465465Fumarate hydratase class IIPRO_0000161304Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi266835.mll8172.

    Structurei

    3D structure databases

    ProteinModelPortaliQ983U5.
    SMRiQ983U5. Positions 7-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni100 – 1023Substrate bindingUniRule annotation
    Regioni131 – 1344B siteUniRule annotation
    Regioni141 – 1433Substrate bindingUniRule annotation
    Regioni189 – 1902Substrate bindingUniRule annotation
    Regioni326 – 3283Substrate 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.

    Q983U5-1 [UniParc]FASTAAdd to Basket

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    MTVAKTRTET DTFGPIEVAA DRYWGAQAQR SLGNFKIGWE KQPASIVRAL    50
    GVVKRAAAEV NMEMKRLDPV VGKAIVDAAQ EVIDGKLNDH FPLVVWQTGS 100
    GTQSNMNANE VISNRAIEML GGVMGSKKPV HPNDHVNMSQ SSNDTYPTAM 150
    HIACAEQVVH HLIPALHHLH KALDAKARAF NHIIKIGRTH TQDATPLTLG 200
    QEFSGYAAQV ASSIKRIEMT LPGLQELAQG GTAVGTGLNA PVGFAEKVAD 250
    RIAAITGIAF VTAPNKFEAL AAHDSMVFSH GAINAAAAAL FKIANDIRFL 300
    GSGPRSGLGE LSLPENEPGS SIMPGKVNPT QCEAMTQVCV QVFGNNAALT 350
    FAGSQGHFEL NVYNPLMAYN FLQSVQLLSD ASVSFTDNCV VGIEAREDNI 400
    KAALDRSLML VTALAPTIGY DNAAKIAKTA HKNGTTLREE ALATGLVSEV 450
    DYDRLVRPED MTHPG 465
    Length:465
    Mass (Da):49,592
    Last modified:October 1, 2001 - v1
    Checksum:i85407C084D9221F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000012 Genomic DNA. Translation: BAB53785.1.
    RefSeqiNP_108324.1. NC_002678.2.
    WP_010915411.1. NC_002678.2.

    Genome annotation databases

    EnsemblBacteriaiBAB53785; BAB53785; BAB53785.
    GeneIDi1230976.
    KEGGimlo:mll8172.
    PATRICi22487309. VBIMesLot2464_6528.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000012 Genomic DNA. Translation: BAB53785.1 .
    RefSeqi NP_108324.1. NC_002678.2.
    WP_010915411.1. NC_002678.2.

    3D structure databases

    ProteinModelPortali Q983U5.
    SMRi Q983U5. Positions 7-464.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 266835.mll8172.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB53785 ; BAB53785 ; BAB53785 .
    GeneIDi 1230976.
    KEGGi mlo:mll8172.
    PATRICi 22487309. VBIMesLot2464_6528.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci MLOT266835:GJ9L-6478-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MAFF303099.

    Entry informationi

    Entry nameiFUMC_RHILO
    AccessioniPrimary (citable) accession number: Q983U5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2001
    Last modified: October 1, 2014
    This is version 74 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