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Q71XE0

- FUMC_LISMF

UniProt

Q71XE0 - FUMC_LISMF

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Listeria monocytogenes serotype 4b (strain F2365)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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
    Ordered Locus Names:LMOf2365_2258
    OrganismiListeria monocytogenes serotype 4b (strain F2365)
    Taxonomic identifieri265669 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
    ProteomesiUP000000563: 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 – 455455Fumarate hydratase class IIPRO_0000161285Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi265669.LMOf2365_2258.

    Structurei

    3D structure databases

    ProteinModelPortaliQ71XE0.
    SMRiQ71XE0. 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.

    Q71XE0-1 [UniParc]FASTAAdd to Basket

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    MERIERDTLG EISVDATKYW GAQTERSKRN FAIGDNPMPI EIIYAFAQLK    50
    KATAKVNAAE GKLSEEKAIA IGQVCDQIIQ GELDEHFPLV VWQTGSGTQS 100
    NMNVNEVIAH VANLTLGEGQ IHPNDDVNMS QSSNDTFPTA MHIAAYGALV 150
    TKLLPEITKM EAVLAEKKSK YMHLVKIGRT HLQDATPLTL GQEISGWEAC 200
    LTNNKNYLET SMKAILPLAI GGTAVGTGLN ASRDFGDKVA EELMKQTGYP 250
    FTSDSNKYFA LTSHSPINFV HGSIRSLASD LMKIANDIRL LASGPRSGIG 300
    ELTIPVNEPG SSIMPGKVNP TQCEAMTMVA AQVMGNDVTI NVAASQGNFE 350
    LNVYKPVIIF NFLESVKLLS DSMRSFRLHC LEGLTANEKV IETKVNDSLM 400
    LVTALNPHIG YEKAAKIAKL AFDENTTLKE AAIKTGFVTE KQFDLWIDPL 450
    KMTNL 455
    Length:455
    Mass (Da):49,635
    Last modified:July 5, 2004 - v1
    Checksum:iF471032E5D146F5C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017262 Genomic DNA. Translation: AAT05025.1.
    RefSeqiWP_010959021.1. NC_002973.6.
    YP_014848.1. NC_002973.6.

    Genome annotation databases

    EnsemblBacteriaiAAT05025; AAT05025; LMOf2365_2258.
    GeneIDi2799834.
    KEGGilmf:LMOf2365_2258.
    PATRICi20325839. VBILisMon105049_2273.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017262 Genomic DNA. Translation: AAT05025.1 .
    RefSeqi WP_010959021.1. NC_002973.6.
    YP_014848.1. NC_002973.6.

    3D structure databases

    ProteinModelPortali Q71XE0.
    SMRi Q71XE0. Positions 3-452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 265669.LMOf2365_2258.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAT05025 ; AAT05025 ; LMOf2365_2258 .
    GeneIDi 2799834.
    KEGGi lmf:LMOf2365_2258.
    PATRICi 20325839. VBILisMon105049_2273.

    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: F2365.

    Entry informationi

    Entry nameiFUMC_LISMF
    AccessioniPrimary (citable) accession number: Q71XE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 72 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