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A1T7Y0

- DUT_MYCVP

UniProt

A1T7Y0 - DUT_MYCVP

Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (06 Feb 2007)
      Previous versions | rss
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    Functioni

    This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.UniRule annotation

    Catalytic activityi

    dUTP + H2O = dUMP + diphosphate.UniRule annotation

    Cofactori

    Magnesium.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei77 – 771SubstrateUniRule annotation
    Binding sitei91 – 911Substrate; via amide nitrogen and carbonyl oxygenUniRule annotation

    GO - Molecular functioni

    1. dUTP diphosphatase activity Source: UniProtKB-HAMAP
    2. magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. dUMP biosynthetic process Source: UniProtKB-UniPathway
    2. dUTP metabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMVAN350058:GIWR-2481-MONOMER.
    UniPathwayiUPA00610; UER00666.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyuridine 5'-triphosphate nucleotidohydrolaseUniRule annotation (EC:3.6.1.23UniRule annotation)
    Short name:
    dUTPaseUniRule annotation
    Alternative name(s):
    dUTP pyrophosphataseUniRule annotation
    Gene namesi
    Name:dutUniRule annotation
    Ordered Locus Names:Mvan_2467
    OrganismiMycobacterium vanbaalenii (strain DSM 7251 / PYR-1)
    Taxonomic identifieri350058 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000009159: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 154154Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_1000015490Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi350058.Mvan_2467.

    Structurei

    3D structure databases

    ProteinModelPortaliA1T7Y0.
    SMRiA1T7Y0. Positions 1-144.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni64 – 663Substrate bindingUniRule annotation
    Regioni81 – 833Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the dUTPase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0756.
    HOGENOMiHOG000028966.
    KOiK01520.
    OMAiFERFDRI.
    OrthoDBiEOG689HXK.

    Family and domain databases

    Gene3Di2.70.40.10. 1 hit.
    HAMAPiMF_00116. dUTPase_bact.
    InterProiIPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    IPR008181. dUTPase_1.
    [Graphical view]
    PfamiPF00692. dUTPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51283. SSF51283. 1 hit.
    TIGRFAMsiTIGR00576. dut. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A1T7Y0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPTTLAVVRL DRDLPLPSRA HDGDAGVDLY SAQDVELAPG QRALVPTGIA    50
    VAIPHGMVGL IHPRSGLAAR VGLSIVNSPG TVDAGYRGEI KVSLINLDPA 100
    APIAIRRGDR IAQLLVQRVE LPELVEVTSF DEAGLADTTR GDGGHGSSGG 150
    HASL 154
    Length:154
    Mass (Da):15,891
    Last modified:February 6, 2007 - v1
    Checksum:iB85EA882E313C3EA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000511 Genomic DNA. Translation: ABM13280.1.
    RefSeqiWP_011779692.1. NC_008726.1.
    YP_953286.1. NC_008726.1.

    Genome annotation databases

    EnsemblBacteriaiABM13280; ABM13280; Mvan_2467.
    GeneIDi4645515.
    KEGGimva:Mvan_2467.
    PATRICi18183195. VBIMycVan31953_2524.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000511 Genomic DNA. Translation: ABM13280.1 .
    RefSeqi WP_011779692.1. NC_008726.1.
    YP_953286.1. NC_008726.1.

    3D structure databases

    ProteinModelPortali A1T7Y0.
    SMRi A1T7Y0. Positions 1-144.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 350058.Mvan_2467.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABM13280 ; ABM13280 ; Mvan_2467 .
    GeneIDi 4645515.
    KEGGi mva:Mvan_2467.
    PATRICi 18183195. VBIMycVan31953_2524.

    Phylogenomic databases

    eggNOGi COG0756.
    HOGENOMi HOG000028966.
    KOi K01520.
    OMAi FERFDRI.
    OrthoDBi EOG689HXK.

    Enzyme and pathway databases

    UniPathwayi UPA00610 ; UER00666 .
    BioCyci MVAN350058:GIWR-2481-MONOMER.

    Family and domain databases

    Gene3Di 2.70.40.10. 1 hit.
    HAMAPi MF_00116. dUTPase_bact.
    InterProi IPR029054. dUTPase-like.
    IPR008180. dUTPase/dCTP_deaminase.
    IPR008181. dUTPase_1.
    [Graphical view ]
    Pfami PF00692. dUTPase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51283. SSF51283. 1 hit.
    TIGRFAMsi TIGR00576. dut. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 7251 / PYR-1.

    Entry informationi

    Entry nameiDUT_MYCVP
    AccessioniPrimary (citable) accession number: A1T7Y0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: February 6, 2007
    Last modified: October 1, 2014
    This is version 54 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Each trimer binds three substrate molecules. The ligands are bound between subunits, and for each substrate molecule, residues from adjacent subunits contribute to the binding interactions By similarity.By similarity

    Keywords - Technical termi

    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