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P33317 (DUT_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxyuridine 5'-triphosphate nucleotidohydrolase

Short name=dUTPase
EC=3.6.1.23
Alternative name(s):
dUTP pyrophosphatase
Gene names
Name:DUT1
Ordered Locus Names:YBR252W
ORF Names:YBR1705
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

dUTP + H2O = dUMP + diphosphate.

Cofactor

Magnesium.

Pathway

Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.

Subunit structure

Homotrimer.

Miscellaneous

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

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.

Sequence similarities

Belongs to the dUTPase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 147147Deoxyuridine 5'-triphosphate nucleotidohydrolase
PRO_0000182937

Regions

Region68 – 703Substrate binding
Region82 – 854Substrate binding
Region142 – 1432Substrate binding

Sites

Binding site931Substrate; via amide nitrogen and carbonyl oxygen
Binding site1371Substrate

Experimental info

Sequence conflict101K → N in CAA52322. Ref.1

Secondary structure

............................... 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33317 [UniParc].

Last modified October 25, 2004. Version 2.
Checksum: 19AC6012C3A061F2

FASTA14715,307
        10         20         30         40         50         60 
MTATSDKVLK IQLRSASATV PTKGSATAAG YDIYASQDIT IPAMGQGMVS TDISFTVPVG 

        70         80         90        100        110        120 
TYGRIAPRSG LAVKNGIQTG AGVVDRDYTG EVKVVLFNHS QRDFAIKKGD RVAQLILEKI 

       130        140 
VDDAQIVVVD SLEESARGAG GFGSTGN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS38189.
RefSeqNP_009811.3. NM_001178600.3.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP33317.
SMRP33317. Positions 6-143.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32947. 47 interactions.
DIPDIP-1661N.
IntActP33317. 3 interactions.
MINTMINT-410177.
STRING4932.YBR252W.

Proteomic databases

PaxDbP33317.
PeptideAtlasP33317.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR252W; YBR252W; YBR252W.
GeneID852554.
KEGGsce:YBR252W.

Organism-specific databases

CYGDYBR252w.
SGDS000000456. DUT1.

Phylogenomic databases

eggNOGCOG0756.
GeneTreeENSGT00390000018390.
HOGENOMHOG000028966.
KOK01520.
OMALVDTQIS.
OrthoDBEOG7T7H6C.

Enzyme and pathway databases

BioCycYEAST:YBR252W-MONOMER.
UniPathwayUPA00610; UER00666.

Gene expression databases

GenevestigatorP33317.

Family and domain databases

InterProIPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00576. dut. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP33317.
NextBio971649.
PROP33317.

Entry information

Entry nameDUT_YEAST
AccessionPrimary (citable) accession number: P33317
Secondary accession number(s): D6VQP8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 25, 2004
Last modified: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways