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

    Gene ID: 850844, updated on 18-Sep-2024

    Summary

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    Official Symbol
    PCD1
    Official Full Name
    8-oxo-dGTP diphosphatase
    Primary source
    SGD:S000004141
    Locus tag
    YLR151C
    See related
    AllianceGenome:SGD:S000004141; FungiDB:YLR151C; VEuPathDB:YLR151C
    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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    See PCD1 in Genome Data Viewer
    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
      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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