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Protein

Deoxyuridine 5'-triphosphate nucleotidohydrolase

Gene

DUT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YBR252W-MONOMER.
ReactomeiREACT_259872. Pyrimidine biosynthesis.
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. 48 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 – 136Combined sources
Beta strandi22 – 254Combined sources
Beta strandi29 – 346Combined sources
Beta strandi39 – 413Combined sources
Beta strandi45 – 506Combined sources
Beta strandi53 – 564Combined sources
Beta strandi61 – 666Combined sources
Helixi69 – 757Combined sources
Beta strandi77 – 793Combined sources
Beta strandi93 – 986Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi111 – 12010Combined sources
Beta strandi125 – 1284Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiLICEKIC.
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

        10         20         30         40         50
MTATSDKVLK IQLRSASATV PTKGSATAAG YDIYASQDIT IPAMGQGMVS
60 70 80 90 100
TDISFTVPVG TYGRIAPRSG LAVKNGIQTG AGVVDRDYTG EVKVVLFNHS
110 120 130 140
QRDFAIKKGD RVAQLILEKI VDDAQIVVVD SLEESARGAG GFGSTGN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi32947. 48 interactions.
DIPiDIP-1661N.
IntActiP33317. 3 interactions.
MINTiMINT-410177.
STRINGi4932.YBR252W.

Proteomic databases

MaxQBiP33317.
PaxDbiP33317.
PeptideAtlasiP33317.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYBR252w.
SGDiS000000456. DUT1.

Phylogenomic databases

eggNOGiCOG0756.
GeneTreeiENSGT00390000018390.
HOGENOMiHOG000028966.
KOiK01520.
OMAiLICEKIC.
OrthoDBiEOG7T7H6C.

Enzyme and pathway databases

UniPathwayiUPA00610; UER00666.
BioCyciYEAST:YBR252W-MONOMER.
ReactomeiREACT_259872. Pyrimidine biosynthesis.

Miscellaneous databases

EvolutionaryTraceiP33317.
NextBioi971649.
PROiP33317.

Gene expression databases

GenevestigatoriP33317.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 130 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.