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P33317

- DUT_YEAST

UniProt

P33317 - DUT_YEAST

Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

DUT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (25 Oct 2004)
      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.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei93 – 931Substrate; via amide nitrogen and carbonyl oxygen
    Binding sitei137 – 1371Substrate

    GO - Molecular functioni

    1. dITP diphosphatase activity Source: SGD
    2. dUTP diphosphatase activity Source: SGD
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. dITP catabolic process Source: SGD
    2. dUMP biosynthetic process Source: UniProtKB-UniPathway
    3. dUTP catabolic process Source: SGD
    4. pyrimidine deoxyribonucleoside triphosphate catabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:YBR252W-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:DUT1
    Ordered Locus Names:YBR252W
    ORF Names:YBR1705
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR252w.
    SGDiS000000456. DUT1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 147147Deoxyuridine 5'-triphosphate nucleotidohydrolasePRO_0000182937Add
    BLAST

    Proteomic databases

    MaxQBiP33317.
    PaxDbiP33317.
    PeptideAtlasiP33317.

    Expressioni

    Gene expression databases

    GenevestigatoriP33317.

    Interactioni

    Subunit structurei

    Homotrimer.

    Protein-protein interaction databases

    BioGridi32947. 47 interactions.
    DIPiDIP-1661N.
    IntActiP33317. 3 interactions.
    MINTiMINT-410177.
    STRINGi4932.YBR252W.

    Structurei

    Secondary structure

    1
    147
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 136
    Beta strandi22 – 254
    Beta strandi29 – 346
    Beta strandi39 – 413
    Beta strandi45 – 506
    Beta strandi53 – 564
    Beta strandi61 – 666
    Helixi69 – 757
    Beta strandi77 – 793
    Beta strandi93 – 986
    Beta strandi100 – 1023
    Beta strandi104 – 1063
    Beta strandi111 – 12010
    Beta strandi125 – 1284
    Beta strandi136 – 1383

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3F4FX-ray2.00A/B/C1-147[»]
    3HHQX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-147[»]
    3P48X-ray1.67A/B/C1-147[»]
    ProteinModelPortaliP33317.
    SMRiP33317. Positions 6-143.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33317.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni68 – 703Substrate binding
    Regioni82 – 854Substrate binding
    Regioni142 – 1432Substrate binding

    Sequence similaritiesi

    Belongs to the dUTPase family.Curated

    Phylogenomic databases

    eggNOGiCOG0756.
    GeneTreeiENSGT00390000018390.
    HOGENOMiHOG000028966.
    KOiK01520.
    OMAiYSRIDFE.
    OrthoDBiEOG7T7H6C.

    Family and domain databases

    Gene3Di2.70.40.10. 1 hit.
    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.

    P33317-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTATSDKVLK IQLRSASATV PTKGSATAAG YDIYASQDIT IPAMGQGMVS    50
    TDISFTVPVG TYGRIAPRSG LAVKNGIQTG AGVVDRDYTG EVKVVLFNHS 100
    QRDFAIKKGD RVAQLILEKI VDDAQIVVVD SLEESARGAG GFGSTGN 147
    Length:147
    Mass (Da):15,307
    Last modified:October 25, 2004 - v2
    Checksum:i19AC6012C3A061F2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101K → N in CAA52322. (PubMed:8223452)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74263 Genomic DNA. Translation: CAA52322.1.
    L20296 Genomic DNA. Translation: AAA65611.1.
    Z36121 Genomic DNA. Translation: CAA85215.1.
    AY693064 Genomic DNA. Translation: AAT93083.1.
    BK006936 Genomic DNA. Translation: DAA07368.1.
    PIRiS38189.
    RefSeqiNP_009811.3. NM_001178600.3.

    Genome annotation databases

    EnsemblFungiiYBR252W; YBR252W; YBR252W.
    GeneIDi852554.
    KEGGisce:YBR252W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74263 Genomic DNA. Translation: CAA52322.1 .
    L20296 Genomic DNA. Translation: AAA65611.1 .
    Z36121 Genomic DNA. Translation: CAA85215.1 .
    AY693064 Genomic DNA. Translation: AAT93083.1 .
    BK006936 Genomic DNA. Translation: DAA07368.1 .
    PIRi S38189.
    RefSeqi NP_009811.3. NM_001178600.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3F4F X-ray 2.00 A/B/C 1-147 [» ]
    3HHQ X-ray 2.00 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1-147 [» ]
    3P48 X-ray 1.67 A/B/C 1-147 [» ]
    ProteinModelPortali P33317.
    SMRi P33317. Positions 6-143.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32947. 47 interactions.
    DIPi DIP-1661N.
    IntActi P33317. 3 interactions.
    MINTi MINT-410177.
    STRINGi 4932.YBR252W.

    Proteomic databases

    MaxQBi P33317.
    PaxDbi P33317.
    PeptideAtlasi P33317.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR252W ; YBR252W ; YBR252W .
    GeneIDi 852554.
    KEGGi sce:YBR252W.

    Organism-specific databases

    CYGDi YBR252w.
    SGDi S000000456. DUT1.

    Phylogenomic databases

    eggNOGi COG0756.
    GeneTreei ENSGT00390000018390.
    HOGENOMi HOG000028966.
    KOi K01520.
    OMAi YSRIDFE.
    OrthoDBi EOG7T7H6C.

    Enzyme and pathway databases

    UniPathwayi UPA00610 ; UER00666 .
    BioCyci YEAST:YBR252W-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P33317.
    NextBioi 971649.
    PROi P33317.

    Gene expression databases

    Genevestigatori P33317.

    Family and domain databases

    Gene3Di 2.70.40.10. 1 hit.
    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. "dUTP pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae."
      Gadsden M.H., McIntosh E.M., Game J.C., Wilson P.J., Haynes R.H.
      EMBO J. 12:4425-4431(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The complete sequence of a 6794 bp segment located on the right arm of chromosome II of Saccharomyces cerevisiae. Finding of a putative dUTPase in a yeast."
      Doignon F., Biteau N., Aigle M., Crouzet M.
      Yeast 9:1131-1137(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDUT_YEAST
    AccessioniPrimary (citable) accession number: P33317
    Secondary accession number(s): D6VQP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: October 25, 2004
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 4340 molecules/cell in log phase SD medium.1 Publication
    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3