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Q9JTR0

- FUMC_NEIMA

UniProt

Q9JTR0 - FUMC_NEIMA

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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 sitei187 – 1871Proton donor/acceptorBy similarity
    Active sitei317 – 3171By similarity
    Binding sitei318 – 3181SubstrateUniRule annotation
    Sitei330 – 3301Important 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

    BioCyciNMEN122587:GI3Q-1519-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:NMA1670
    OrganismiNeisseria meningitidis serogroup A / serotype 4A (strain Z2491)
    Taxonomic identifieri122587 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000000626: 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 – 462462Fumarate hydratase class IIPRO_0000161291Add
    BLAST

    Proteomic databases

    PRIDEiQ9JTR0.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi122587.NMA1670.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JTR0.
    SMRiQ9JTR0. Positions 4-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 993Substrate bindingUniRule annotation
    Regioni128 – 1314B siteUniRule annotation
    Regioni138 – 1403Substrate bindingUniRule annotation
    Regioni186 – 1872Substrate bindingUniRule annotation
    Regioni323 – 3253Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061737.
    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.

    Q9JTR0-1 [UniParc]FASTAAdd to Basket

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    MNTRTEHDTM GNVEVPSEAY WGAQTQRSRN NFKIGGETLP QPLIYALALV    50
    KKAAAATNVS LGRIKPEQAD LITQAADDVL NGKLDGQFPL VVWQTGSGTQ 100
    SNMNMNEVLA NRANEIAGTG LAAYQPVHPN DHVNHAQSTN DAFPTAIHVA 150
    AAIEINRHLI PAVKALRDTL DKKAQAFAPI VKIGRTHLQD ATPLTLGQEF 200
    SGYVSQLDHG LGRLNDALKD LYELALGGTA VGTGLNSHPE YAEKAAAKLA 250
    ELSGLPFVSA PNKFEALGGR DAAVAASGAL KTLAASLNKI ANDIRWLASG 300
    PRCGLGEIKI PENEPGSSIM PGKVNPTQCE AMTMVCCQVF GNDVTIGMAG 350
    ASGNFELNVY MPVIAYNLLQ SIRLLGDACN SFNEHCAVGI EPVPEKIDYF 400
    LHHSLMLVTA LNRKIGYENA AKVAKTAYKN NKSLRETAVE LGLLTGEEFD 450
    ELVVPADMVH PR 462
    Length:462
    Mass (Da):49,391
    Last modified:October 1, 2000 - v1
    Checksum:i6F63B3D506E26C85
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL157959 Genomic DNA. Translation: CAM08803.1.
    PIRiB81862.
    RefSeqiYP_002342970.1. NC_003116.1.

    Genome annotation databases

    EnsemblBacteriaiCAM08803; CAM08803; NMA1670.
    GeneIDi908059.
    KEGGinma:NMA1670.
    PATRICi20364519. VBINeiMen132687_1961.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL157959 Genomic DNA. Translation: CAM08803.1 .
    PIRi B81862.
    RefSeqi YP_002342970.1. NC_003116.1.

    3D structure databases

    ProteinModelPortali Q9JTR0.
    SMRi Q9JTR0. Positions 4-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 122587.NMA1670.

    Proteomic databases

    PRIDEi Q9JTR0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAM08803 ; CAM08803 ; NMA1670 .
    GeneIDi 908059.
    KEGGi nma:NMA1670.
    PATRICi 20364519. VBINeiMen132687_1961.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061737.
    KOi K01679.
    OMAi MESFNIH.
    OrthoDBi EOG6V1M4M.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci NMEN122587:GI3Q-1519-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: Z2491.

    Entry informationi

    Entry nameiFUMC_NEIMA
    AccessioniPrimary (citable) accession number: Q9JTR0
    Secondary accession number(s): A1ISP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 87 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