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P0A553

- DUT_MYCBO

UniProt

P0A553 - DUT_MYCBO

Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      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

    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:Mb2716c
    OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
    Taxonomic identifieri233413 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001419: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 154154Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_0000182881Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi233413.Mb2716c.

    Structurei

    3D structure databases

    ProteinModelPortaliP0A553.
    SMRiP0A553. Positions 1-138.
    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.

    P0A553-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTTLAIVRL DPGLPLPSRA HDGDAGVDLY SAEDVELAPG RRALVRTGVA    50
    VAVPFGMVGL VHPRSGLATR VGLSIVNSPG TIDAGYRGEI KVALINLDPA 100
    APIVVHRGDR IAQLLVQRVE LVELVEVSSF DEAGLASTSR GDGGHGSSGG 150
    HASL 154
    Length:154
    Mass (Da):15,803
    Last modified:March 15, 2005 - v1
    Checksum:i836D5E6420EF455B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248333 Genomic DNA. Translation: CDO43980.1.
    RefSeqiNP_856362.1. NC_002945.3.

    Genome annotation databases

    EnsemblBacteriaiCAD94901; CAD94901; Mb2716c.
    GeneIDi1091895.
    KEGGimbo:Mb2716c.
    PATRICi18007691. VBIMycBov88188_2978.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248333 Genomic DNA. Translation: CDO43980.1 .
    RefSeqi NP_856362.1. NC_002945.3.

    3D structure databases

    ProteinModelPortali P0A553.
    SMRi P0A553. Positions 1-138.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 233413.Mb2716c.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD94901 ; CAD94901 ; Mb2716c .
    GeneIDi 1091895.
    KEGGi mbo:Mb2716c.
    PATRICi 18007691. VBIMycBov88188_2978.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00610 ; UER00666 .

    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: ATCC BAA-935 / AF2122/97.

    Entry informationi

    Entry nameiDUT_MYCBO
    AccessioniPrimary (citable) accession number: P0A553
    Secondary accession number(s): O07199, X2BLL2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 57 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

    Documents

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

    External Data

    Dasty 3