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P06968

- DUT_ECOLI

UniProt

P06968 - DUT_ECOLI

Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

dut

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      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.

    Catalytic activityi

    dUTP + H2O = dUMP + diphosphate.

    Cofactori

    Magnesium.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei83 – 831Substrate1 Publication
    Binding sitei97 – 971Substrate; via amide nitrogen and carbonyl oxygen1 Publication

    GO - Molecular functioni

    1. dUTP diphosphatase activity Source: EcoCyc
    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

    BioCyciEcoCyc:DUTP-PYROP-MONOMER.
    ECOL316407:JW3615-MONOMER.
    MetaCyc:DUTP-PYROP-MONOMER.
    UniPathwayiUPA00610; UER00666.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyuridine 5'-triphosphate nucleotidohydrolase (EC:3.6.1.23)
    Short name:
    dUTPase
    Alternative name(s):
    dUTP pyrophosphatase
    Gene namesi
    Name:dut
    Synonyms:dnaS, sof
    Ordered Locus Names:b3640, JW3615
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10251. dut.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi89 – 891D → N: Reduces catalytic activity 40000-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 151151Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_0000182858Add
    BLAST

    Proteomic databases

    PaxDbiP06968.
    PRIDEiP06968.

    2D gel databases

    SWISS-2DPAGEP06968.

    Expressioni

    Gene expression databases

    GenevestigatoriP06968.

    Interactioni

    Subunit structurei

    Homotrimer.1 Publication

    Protein-protein interaction databases

    IntActiP06968. 11 interactions.
    MINTiMINT-1279301.
    STRINGi511145.b3640.

    Structurei

    Secondary structure

    1
    151
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84
    Turni11 – 155
    Beta strandi30 – 334
    Beta strandi40 – 423
    Beta strandi47 – 5711
    Beta strandi63 – 697
    Helixi71 – 777
    Beta strandi79 – 813
    Beta strandi84 – 885
    Beta strandi94 – 1029
    Beta strandi104 – 1063
    Beta strandi108 – 1103
    Beta strandi115 – 1239

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DUDX-ray2.30A1-151[»]
    1DUPX-ray1.90A1-151[»]
    1EU5X-ray1.45A1-151[»]
    1EUWX-ray1.05A1-151[»]
    1RN8X-ray1.93A1-151[»]
    1RNJX-ray1.70A1-151[»]
    1SEHX-ray1.47A1-151[»]
    1SYLX-ray1.95A1-151[»]
    2HR6X-ray1.84A1-151[»]
    2HRMX-ray1.70A1-151[»]
    DisProtiDP00337.
    ProteinModelPortaliP06968.
    SMRiP06968. Positions 1-135.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06968.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni70 – 723Substrate bindingBy similarity
    Regioni87 – 893Substrate bindingCurated

    Sequence similaritiesi

    Belongs to the dUTPase family.Curated

    Phylogenomic databases

    eggNOGiCOG0756.
    HOGENOMiHOG000028968.
    KOiK01520.
    OMAiSIYIGDP.
    OrthoDBiEOG689HXK.
    PhylomeDBiP06968.

    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.

    P06968-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKIDVKILD PRVGKEFPLP TYATSGSAGL DLRACLNDAV ELAPGDTTLV    50
    PTGLAIHIAD PSLAAMMLPR SGLGHKHGIV LGNLVGLIDS DYQGQLMISV 100
    WNRGQDSFTI QPGERIAQMI FVPVVQAEFN LVEDFDATDR GEGGFGHSGR 150
    Q 151
    Length:151
    Mass (Da):16,155
    Last modified:April 1, 1988 - v1
    Checksum:i98FA3DE0BC70FFB2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01714 Genomic DNA. Translation: CAA25859.1.
    V01578 Genomic DNA. Translation: CAA24897.1.
    L10328 Genomic DNA. Translation: AAA61993.1.
    U00096 Genomic DNA. Translation: AAC76664.1.
    AP009048 Genomic DNA. Translation: BAE77652.1.
    PIRiA30388. WPECDU.
    RefSeqiNP_418097.1. NC_000913.3.
    YP_491793.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76664; AAC76664; b3640.
    BAE77652; BAE77652; BAE77652.
    GeneIDi12934430.
    948607.
    KEGGiecj:Y75_p3534.
    eco:b3640.
    PATRICi32122767. VBIEscCol129921_3760.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01714 Genomic DNA. Translation: CAA25859.1 .
    V01578 Genomic DNA. Translation: CAA24897.1 .
    L10328 Genomic DNA. Translation: AAA61993.1 .
    U00096 Genomic DNA. Translation: AAC76664.1 .
    AP009048 Genomic DNA. Translation: BAE77652.1 .
    PIRi A30388. WPECDU.
    RefSeqi NP_418097.1. NC_000913.3.
    YP_491793.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DUD X-ray 2.30 A 1-151 [» ]
    1DUP X-ray 1.90 A 1-151 [» ]
    1EU5 X-ray 1.45 A 1-151 [» ]
    1EUW X-ray 1.05 A 1-151 [» ]
    1RN8 X-ray 1.93 A 1-151 [» ]
    1RNJ X-ray 1.70 A 1-151 [» ]
    1SEH X-ray 1.47 A 1-151 [» ]
    1SYL X-ray 1.95 A 1-151 [» ]
    2HR6 X-ray 1.84 A 1-151 [» ]
    2HRM X-ray 1.70 A 1-151 [» ]
    DisProti DP00337.
    ProteinModelPortali P06968.
    SMRi P06968. Positions 1-135.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P06968. 11 interactions.
    MINTi MINT-1279301.
    STRINGi 511145.b3640.

    2D gel databases

    SWISS-2DPAGE P06968.

    Proteomic databases

    PaxDbi P06968.
    PRIDEi P06968.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76664 ; AAC76664 ; b3640 .
    BAE77652 ; BAE77652 ; BAE77652 .
    GeneIDi 12934430.
    948607.
    KEGGi ecj:Y75_p3534.
    eco:b3640.
    PATRICi 32122767. VBIEscCol129921_3760.

    Organism-specific databases

    EchoBASEi EB0247.
    EcoGenei EG10251. dut.

    Phylogenomic databases

    eggNOGi COG0756.
    HOGENOMi HOG000028968.
    KOi K01520.
    OMAi SIYIGDP.
    OrthoDBi EOG689HXK.
    PhylomeDBi P06968.

    Enzyme and pathway databases

    UniPathwayi UPA00610 ; UER00666 .
    BioCyci EcoCyc:DUTP-PYROP-MONOMER.
    ECOL316407:JW3615-MONOMER.
    MetaCyc:DUTP-PYROP-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P06968.
    PROi P06968.

    Gene expression databases

    Genevestigatori P06968.

    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. "Nucleotide sequence of the structural gene for dUTPase of Escherichia coli K-12."
      Lundberg L.G., Thoresson H.-O., Karlstroem O.H., Nyman P.O.
      EMBO J. 2:967-971(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
      Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
      Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    6. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    7. "Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP)."
      Larsson G., Svensson L.A., Nyman P.O.
      Nat. Struct. Biol. 3:532-538(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    8. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    9. "Atomic resolution structure of Escherichia coli dUTPase determined ab initio."
      Gonzalez A., Larsson G., Persson R., Cedergren-Zeppezauer E.S.
      Acta Crystallogr. D 57:767-774(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
    10. "Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase."
      Barabas O., Pongracz V., Kovari J., Wilmanns M., Vertessy B.G.
      J. Biol. Chem. 279:42907-42915(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND SUBSTRATE, COFACTOR, MUTAGENESIS OF ASP-89, SUBUNIT.

    Entry informationi

    Entry nameiDUT_ECOLI
    AccessioniPrimary (citable) accession number: P06968
    Secondary accession number(s): Q2M7V4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 140 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3