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P33317

- DUT_YEAST

UniProt

P33317 - DUT_YEAST

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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: 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

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
Complete GO annotation...

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. 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 – 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

        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:
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. 48 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

« 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: October 29, 2014
This is version 127 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