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Q0SYG7

- DUT_SHIF8

UniProt

Q0SYG7 - DUT_SHIF8

Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Shigella flexneri serotype 5b (strain 8401)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (05 Sep 2006)
      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 sitei83 – 831SubstrateUniRule annotation
    Binding sitei97 – 971Substrate; 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

    BioCyciSFLE373384:GHZM-3886-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:SFV_3890
    OrganismiShigella flexneri serotype 5b (strain 8401)
    Taxonomic identifieri373384 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
    ProteomesiUP000000659: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 151151Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_1000015522Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi373384.SFV_3890.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0SYG7.
    SMRiQ0SYG7. Positions 1-138.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni70 – 723Substrate bindingUniRule annotation
    Regioni87 – 893Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the dUTPase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0756.
    HOGENOMiHOG000028968.
    KOiK01520.
    OMAiSIYIGDP.
    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.

    Q0SYG7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKIDVKILD PRVRKEFPLP TYATSGSAGL DLRACLDDAV ELAPGDTTLV    50
    PTGLAIHIAD PSLAAMMLPR SGLGHKHGIV LGNLVGLIDS DYQGQLMISV 100
    WNRGQDSFTI QPGERIAQMI FVPVVQAEFN LVEDFDATDR GEGGFGHSGR 150
    Q 151
    Length:151
    Mass (Da):16,256
    Last modified:September 5, 2006 - v1
    Checksum:i33413AF66BAB9214
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000266 Genomic DNA. Translation: ABF05898.1.
    RefSeqiYP_691203.1. NC_008258.1.

    Genome annotation databases

    EnsemblBacteriaiABF05898; ABF05898; SFV_3890.
    GeneIDi4210266.
    KEGGisfv:SFV_3890.
    PATRICi18731965. VBIShiFle33408_4420.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000266 Genomic DNA. Translation: ABF05898.1 .
    RefSeqi YP_691203.1. NC_008258.1.

    3D structure databases

    ProteinModelPortali Q0SYG7.
    SMRi Q0SYG7. Positions 1-138.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 373384.SFV_3890.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABF05898 ; ABF05898 ; SFV_3890 .
    GeneIDi 4210266.
    KEGGi sfv:SFV_3890.
    PATRICi 18731965. VBIShiFle33408_4420.

    Phylogenomic databases

    eggNOGi COG0756.
    HOGENOMi HOG000028968.
    KOi K01520.
    OMAi SIYIGDP.
    OrthoDBi EOG689HXK.

    Enzyme and pathway databases

    UniPathwayi UPA00610 ; UER00666 .
    BioCyci SFLE373384:GHZM-3886-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. "Complete genome sequence of Shigella flexneri 5b and comparison with Shigella flexneri 2a."
      Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.
      BMC Genomics 7:173-173(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 8401.

    Entry informationi

    Entry nameiDUT_SHIF8
    AccessioniPrimary (citable) accession number: Q0SYG7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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