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Q929E8

- FUMC_LISIN

UniProt

Q929E8 - FUMC_LISIN

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Listeria innocua serovar 6a (strain CLIP 11262)
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 1 (01 Dec 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 sitei181 – 1811Proton donor/acceptorBy similarity
    Active sitei311 – 3111By similarity
    Binding sitei312 – 3121SubstrateUniRule annotation
    Sitei324 – 3241Important 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

    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:citG
    Ordered Locus Names:lin2328
    OrganismiListeria innocua serovar 6a (strain CLIP 11262)
    Taxonomic identifieri272626 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
    ProteomesiUP000002513: Chromosome

    Organism-specific databases

    GenoListiLIN2328.

    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 – 455455Fumarate hydratase class IIPRO_0000161284Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272626.lin2328.

    Structurei

    3D structure databases

    ProteinModelPortaliQ929E8.
    SMRiQ929E8. Positions 3-452.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni96 – 983Substrate bindingUniRule annotation
    Regioni122 – 1254B siteUniRule annotation
    Regioni132 – 1343Substrate bindingUniRule annotation
    Regioni180 – 1812Substrate bindingUniRule annotation
    Regioni317 – 3193Substrate 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.

    Q929E8-1 [UniParc]FASTAAdd to Basket

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    MERIERDTLG EISVDATKYW GAQTERSRRN FAIGDNYMPK EIIYAFAQLK    50
    KAAAKVNALE GKLSEAKSVA IGNVCDQIIQ GELDEHFPLV VWQTGSGTQS 100
    NMNVNEVIAH VANLTLGEEK VHPNDDVNMS QSSNDTFPTA MHIAAYQALV 150
    TKLLSEITKM EEVLTTKKNQ YMQLVKIGRT HLQDATPLTL GQEISGWEAC 200
    LTNNKNYLES SMKAILPLAI GGTAVGTGLN ASKDFGDKVA EELRKQTGYP 250
    FTSDSNKYFA LTSHSPINFV HGAIRSLASD LMKIANDIRL LASGPRSGIG 300
    ELTLPANEPG SSIMPGKVNP TQCEAITMVA AQVMGNDTTI NIAASQGNFE 350
    LNVYKPVIIF NFLESITLLS DSMRSFRIHC LEGLTANESV IEAKVNDSLM 400
    LVTALNPHIG YEKAAKIAKL AFDENTTLKE AAIKTGFVTE KEFDLWIDPL 450
    KMTNL 455
    Length:455
    Mass (Da):49,737
    Last modified:December 1, 2001 - v1
    Checksum:i800F577E7E5BEB38
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL596171 Genomic DNA. Translation: CAC97556.1.
    PIRiAD1723.
    RefSeqiNP_471660.1. NC_003212.1.
    WP_010991129.1. NC_003212.1.

    Genome annotation databases

    EnsemblBacteriaiCAC97556; CAC97556; CAC97556.
    GeneIDi1131082.
    KEGGilin:lin2328.
    PATRICi20301493. VBILisInn102668_2379.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL596171 Genomic DNA. Translation: CAC97556.1 .
    PIRi AD1723.
    RefSeqi NP_471660.1. NC_003212.1.
    WP_010991129.1. NC_003212.1.

    3D structure databases

    ProteinModelPortali Q929E8.
    SMRi Q929E8. Positions 3-452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272626.lin2328.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC97556 ; CAC97556 ; CAC97556 .
    GeneIDi 1131082.
    KEGGi lin:lin2328.
    PATRICi 20301493. VBILisInn102668_2379.

    Organism-specific databases

    GenoListi LIN2328.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .

    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: CLIP 11262.

    Entry informationi

    Entry nameiFUMC_LISIN
    AccessioniPrimary (citable) accession number: Q929E8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 80 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3