P33317 (DUT_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 116.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Deoxyuridine 5'-triphosphate nucleotidohydrolase Short name=dUTPase EC=3.6.1.23 Alternative name(s): dUTP pyrophosphatase | ||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome] | ||||||
| Taxonomic identifier | 559292 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › ![]() |
Protein attributes
| Sequence length | 147 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Nucleotide metabolism |
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | dITP catabolic process Inferred from direct assay PubMed 21548881. Source: SGD dUMP biosynthetic processInferred from electronic annotation. Source: UniProtKB-UniPathway dUTP catabolic processInferred from direct assay PubMed 21548881. Source: SGD |
| Cellular_component | cytoplasm Inferred from direct assay PubMed 14562095. Source: SGD nucleusInferred from direct assay PubMed 14562095. Source: SGD |
| Molecular_function | dITP diphosphatase activity Inferred from direct assay PubMed 21548881. Source: SGD dUTP diphosphatase activityInferred from direct assay PubMed 21548881. Source: SGD metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 147 | 147 | Deoxyuridine 5'-triphosphate nucleotidohydrolase | PRO_0000182937 | |||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||
| Region | 68 – 70 | 3 | Substrate binding | ||||||||||||||||||||||||||||||||||||
| Region | 82 – 85 | 4 | Substrate binding | ||||||||||||||||||||||||||||||||||||
| Region | 142 – 143 | 2 | Substrate binding | ||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||
| Binding site | 93 | 1 | Substrate; via amide nitrogen and carbonyl oxygen | ||||||||||||||||||||||||||||||||||||
| Binding site | 137 | 1 | Substrate | ||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||
| Modified residue | 89 | 1 | Phosphothreonine Ref.7 Ref.8 | ||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 10 | 1 | K → N in CAA52322. Ref.1 | ||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||
| Beta strand | 8 – 13 | 6 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 22 – 25 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 29 – 34 | 6 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 39 – 41 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 45 – 50 | 6 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 53 – 56 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 61 – 66 | 6 | |||||||||||||||||||||||||||||||||||||
| Helix | 69 – 75 | 7 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 77 – 79 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 93 – 98 | 6 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 100 – 102 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 104 – 106 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 111 – 120 | 10 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 125 – 128 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 136 – 138 | 3 | |||||||||||||||||||||||||||||||||||||
Sequences
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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. 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. 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] | "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-89, MASS SPECTROMETRY. |
| [8] | "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-89, MASS SPECTROMETRY. |
| + | 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. | ||||||||||||||||||||||||
| PIR | S38189. | ||||||||||||||||||||||||
| RefSeq | NP_009811.3. NM_001178600.3. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P33317. | ||||||||||||||||||||||||
| SMR | P33317. Positions 6-143. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| DIP | DIP-1661N. | ||||||||||||||||||||||||
| IntAct | P33317. 4 interactions. | ||||||||||||||||||||||||
| MINT | MINT-410177. | ||||||||||||||||||||||||
| STRING | 4932.YBR252W. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PaxDb | P33317. | ||||||||||||||||||||||||
| PeptideAtlas | P33317. | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| EnsemblFungi | YBR252W; YBR252W; YBR252W. | ||||||||||||||||||||||||
| GeneID | 852554. | ||||||||||||||||||||||||
| KEGG | sce:YBR252W. sce:YBR255C-A. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| CYGD | YBR252w. | ||||||||||||||||||||||||
| SGD | S000000456. DUT1. | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| eggNOG | COG0756. | ||||||||||||||||||||||||
| GeneTree | ENSGT00390000018390. | ||||||||||||||||||||||||
| HOGENOM | HOG000028966. | ||||||||||||||||||||||||
| KO | K01520. | ||||||||||||||||||||||||
| OMA | KVCLINH. | ||||||||||||||||||||||||
| OrthoDB | EOG47M57F. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| UniPathway | UPA00610; UER00666. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| Genevestigator | P33317. | ||||||||||||||||||||||||
| GermOnline | YBR252W. Saccharomyces cerevisiae. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR008180. dUTP_pyroPase. IPR008181. dUTP_pyroPase_sf. [Graphical view] | ||||||||||||||||||||||||
| PANTHER | PTHR11241. PTHR11241. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF00692. dUTPase. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| TIGRFAMs | TIGR00576. dut. 1 hit. | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other | |||||||||||||||||||||||||
| EvolutionaryTrace | P33317. | ||||||||||||||||||||||||
| NextBio | 971649. | ||||||||||||||||||||||||
Entry information
| Entry name | DUT_YEAST | ||||||||
| Accession | Primary (citable) accession number: P33317 Secondary accession number(s): D6VQP8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome II Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
