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PCD1 8-oxo-dGTP diphosphatase [ Saccharomyces cerevisiae S288C ]

Gene ID: 850844, updated on 11-Apr-2024

Summary

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Gene symbol
PCD1
Gene description
8-oxo-dGTP diphosphatase
Primary source
SGD:S000004141
Locus tag
YLR151C
See related
AllianceGenome:SGD:S000004141
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity and CoA pyrophosphatase activity. Involved in DNA repair. Located in peroxisome. Orthologous to several human genes including NUDT7 (nudix hydrolase 7). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:
chromosome: XII
Exon count:
1
Sequence:
Chromosome: XII; NC_001144.5 (441715..442737, complement)

Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene Gid11p Neighboring gene Stm1p Neighboring gene uncharacterized protein Neighboring gene acetate--CoA ligase ACS2

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001144.5

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. A novel Nudix hydrolase for oxidized purine nucleoside triphosphates encoded by ORFYLR151c (PCD1 gene) in Saccharomyces cerevisiae. Nunoshiba T, et al. Nucleic Acids Res, 2004. PMID 15475388, Free PMC Article
  2. The Saccharomyces cerevisiae PCD1 gene encodes a peroxisomal nudix hydrolase active toward coenzyme A and its derivatives. Cartwright JL, et al. J Biol Chem, 2000 Oct 20. PMID 10922370
  3. Multiple Nudix family proteins possess mRNA decapping activity. Song MG, et al. RNA, 2013 Mar. PMID 23353937, Free PMC Article
  4. Increased biosynthesis of acetyl-CoA in the yeast Saccharomyces cerevisiae by overexpression of a deregulated pantothenate kinase gene and engineering of the coenzyme A biosynthetic pathway. Olzhausen J, et al. Appl Microbiol Biotechnol, 2021 Oct. PMID 34491400, Free PMC Article
  5. Heterozygous mutations cause genetic instability in a yeast model of cancer evolution. Coelho MC, et al. Nature, 2019 Feb. PMID 30700905, Free PMC Article

See all (23) citations in PubMed

GeneRIFs: Gene References Into Functions

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables 2-hydroxy-dATP hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity IEA
Inferred from Electronic Annotation
more info
  
enables 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables coenzyme A diphosphatase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables coenzyme A diphosphatase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables magnesium ion binding IEA
Inferred from Electronic Annotation
more info
  
enables manganese ion binding IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in DNA repair IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in coenzyme A catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in nucleoside diphosphate metabolic process IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytosol HDA PubMed 
located_in peroxisome IDA
Inferred from Direct Assay
more info
 PubMed 
located_in peroxisome IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
8-oxo-dGTP diphosphatase
NP_013252.1
  • 8-oxo-dGTP diphosphatase; prevents spontaneous mutagenesis via sanitization of oxidized purine nucleoside triphosphates; can also act as peroxisomal pyrophosphatase with specificity for coenzyme A and CoA derivatives, may function to remove potentially toxic oxidized CoA disulfide from peroxisomes to maintain the capacity for beta-oxidation of fatty acids; nudix hydrolase family member; similar E. coli MutT and human, rat and mouse MTH1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001144.5 Reference assembly

    Range
    441715..442737 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001182038.1 → NP_013252.1  TPA: 8-oxo-dGTP diphosphatase [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_013252.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VYE6, Q12524
    UniProtKB/TrEMBL
    A0A8H4F9W3, A7A150, B3LTB2, B5VN79, C7GMK3, C8ZDC2, G2WIZ0
    Conserved Domains (1) summary
    cd03426
    Location:38 → 265
    CoAse; Coenzyme A pyrophosphatase (CoAse), a member of the Nudix hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative ...
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q12524.1

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