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    ndx-8 Peroxisomal coenzyme A diphosphatase ndx-8 [ Caenorhabditis elegans ]

    Gene ID: 190780, updated on 9-Dec-2024

    Summary

    Official Symbol
    ndx-8
    Official Full Name
    Peroxisomal coenzyme A diphosphatase ndx-8
    Primary source
    WormBase:WBGene00003585
    Locus tag
    CELE_Y87G2A.14
    See related
    AllianceGenome:WB:WBGene00003585
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Caenorhabditis elegans (strain: Bristol N2)
    Lineage
    Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
    Summary
    Enables coenzyme A diphosphatase activity; hydroxymethylglutaryl-CoA hydrolase activity; and succinyl-CoA hydrolase activity. Involved in coenzyme A catabolic process. Predicted to be located in peroxisome. Orthologous to human NUDT7 (nudix hydrolase 7). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

    See ndx-8 in Genome Data Viewer
    Location:
    chromosome: I
    Exon count:
    7
    Sequence:
    Chromosome: I; NC_003279.8 (13492983..13507068)

    Chromosome I - NC_003279.8Genomic Context describing neighboring genes Neighboring gene E3 ubiquitin-protein ligase UBR7;RING-type E3 ubiquitin transferase Neighboring gene S-formylglutathione hydrolase Neighboring gene Protein soem-1 Neighboring gene LITAF domain-containing protein Neighboring gene LITAF domain-containing protein Neighboring gene miscRNA

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Markers

    Gene Ontology Provided by WormBase

    Function Evidence Code Pubs
    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 hydroxymethylglutaryl-CoA hydrolase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables succinyl-CoA hydrolase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Process Evidence Code Pubs
    involved_in coenzyme A catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    involved_in coenzyme A catabolic process IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Component Evidence Code Pubs
    located_in intracellular organelle IDA
    Inferred from Direct Assay
    more info
    PubMed 
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
     
    located_in peroxisomal membrane IEA
    Inferred from Electronic Annotation
    more info
     
    located_in peroxisome IEA
    Inferred from Electronic Annotation
    more info
     
    located_in peroxisome ISS
    Inferred from Sequence or Structural Similarity
    more info
    PubMed 

    General protein information

    Preferred Names
    Peroxisomal coenzyme A diphosphatase ndx-8
    NP_493372.1
    • Confirmed by transcript evidence

    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_003279.8 Reference assembly

      Range
      13492983..13507068
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_060971.3NP_493372.1  Peroxisomal coenzyme A diphosphatase ndx-8 [Caenorhabditis elegans]

      See identical proteins and their annotated locations for NP_493372.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      Q9NA25
      Conserved Domains (1) summary
      cd03426
      Location:28182
      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 ...