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Q7V5R2

- FUMC_PROMM

UniProt

Q7V5R2 - FUMC_PROMM

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Prochlorococcus marinus (strain MIT 9313)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      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

    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:PMT_1485
    OrganismiProchlorococcus marinus (strain MIT 9313)
    Taxonomic identifieri74547 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
    ProteomesiUP000001423: 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 – 466466Fumarate hydratase class IIPRO_0000161297Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi74547.PMT1485.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7V5R2.
    SMRiQ7V5R2. Positions 6-461.
    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.
    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.

    Q7V5R2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMADLMRIEH DSMGTIEVPA GVLWGAQTQR SLLNFAISTD RMPVELIHAL    50
    ALIKQAAASV NCRLGVLDEV QRDQIIKAAS AVASGLHDDQ FPLRVWQTGS 100
    GTHTNMNVNE VISNLASQAN DEPLGSHRPV HPNDHVNRSQ STNDAFPTAI 150
    HIAAVQGITN NLLPELEQLI AAFARKSDAW SDIIKIGRTH LQDAVPLTLG 200
    QEASAWRDQI ASAHSRIQSS LIELYPLPLG GTAVGTGLNA PARFGQETAA 250
    QLASITGLPF SSAKNKFAVM ASHDGLVNAM AQLRMLAVAL FKISNDLRLL 300
    ACGPRAGLAE LHLPENEPGS SIMPGKVNPS QCEAMAMVCL QVIGLDSAVT 350
    MAGGSGHLQM NVYKPLIGFN LLHSIELLHD ACRKYRLAMV QGIEPNRIKI 400
    QHDLEQSLML VTALAPEIGY DKASEIAHLA HEKGFSLREA ALKLGYVSKE 450
    DFDRIVNPAL MTSARL 466
    Length:466
    Mass (Da):50,233
    Last modified:October 1, 2003 - v1
    Checksum:i395908D8DD84B12D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX548175 Genomic DNA. Translation: CAE21660.1.
    RefSeqiNP_895312.1. NC_005071.1.
    WP_011130853.1. NC_005071.1.

    Genome annotation databases

    EnsemblBacteriaiCAE21660; CAE21660; PMT_1485.
    GeneIDi1728513.
    KEGGipmt:PMT1485.
    PATRICi23011523. VBIProMar135351_1905.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX548175 Genomic DNA. Translation: CAE21660.1 .
    RefSeqi NP_895312.1. NC_005071.1.
    WP_011130853.1. NC_005071.1.

    3D structure databases

    ProteinModelPortali Q7V5R2.
    SMRi Q7V5R2. Positions 6-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 74547.PMT1485.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAE21660 ; CAE21660 ; PMT_1485 .
    GeneIDi 1728513.
    KEGGi pmt:PMT1485.
    PATRICi 23011523. VBIProMar135351_1905.

    Phylogenomic databases

    eggNOGi COG0114.
    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: MIT 9313.

    Entry informationi

    Entry nameiFUMC_PROMM
    AccessioniPrimary (citable) accession number: Q7V5R2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 75 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