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    CTA1 catalase A [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851843, updated on 17-May-2024

    Summary

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    Gene symbol
    CTA1
    Gene description
    catalase A
    Primary source
    FungiDB:YDR256C
    Locus tag
    YDR256C
    See related
    SGD:S000002664; AllianceGenome:SGD:S000002664; VEuPathDB:YDR256C
    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 catalase activity. Involved in age-dependent response to reactive oxygen species and hydrogen peroxide catabolic process. Located in mitochondrial matrix and peroxisomal matrix. Human ortholog(s) of this gene implicated in several diseases, including acatalasia; eye disease (multiple); lung disease (multiple); osteonecrosis; and pseudoxanthoma elasticum. Orthologous to human CAT (catalase). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See CTA1 in Genome Data Viewer
    Location:
    chromosome: IV
    Exon count:
    1
    Sequence:
    Chromosome: IV; NC_001136.10 (968133..969680, complement)

    Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene Chl4p Neighboring gene ubiquitin-protein ligase RMD5 Neighboring gene ribosomal lysine N-methyltransferase Neighboring gene chaperone ATPase HSP78

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001136.10

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Oxidative stress response to menadione and cumene hydroperoxide in the opportunistic fungal pathogen Candida glabrata. Cuéllar-Cruz M, et al. Mem Inst Oswaldo Cruz, 2009 Jul. PMID 19722092
    2. Dual targeting of yeast catalase A to peroxisomes and mitochondria. Petrova VY, et al. Biochem J, 2004 Jun 1. PMID 14998369, Free PMC Article
    3. Structure of catalase-A from Saccharomyces cerevisiae. Maté MJ, et al. J Mol Biol, 1999 Feb 12. PMID 9931255
    4. Crystallization and preliminary structural analysis of catalase A from Saccharomyces cerevisiae. Berthet S, et al. Protein Sci, 1997 Feb. PMID 9041655, Free PMC Article
    5. A Saccharomyces cerevisiae upstream activating sequence mediates induction of peroxisome proliferation by fatty acids. Filipits M, et al. Gene, 1993 Sep 30. PMID 8406042

    See all (93) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The Ile264 amino acid residue in Pex5, which is adjacent to the FxxxW diaromatic domain that was previously shown to be crucial for recognizing AOx and Cat2 as cargos, is also important for the efficient import of Fox2 and Cta1.
      Title: The budding yeast Pex5p receptor directs Fox2p and Cta1p into peroxisomes via its N-terminal region near the FxxxW domain.
    2. MET18 deficiency diminished the replicative capacity of yeast cells as evidenced by the shortened replicative lifespan, which can be restored by CTT1 overexpression, but not by CTA1, in the MET18-deficient cells.
      Title: MET18 Deficiency Increases the Sensitivity of Yeast to Oxidative Stress and Shortens Replicative Lifespan by Inhibiting Catalase Activity.
    3. Ccp1 responds to respiration-derived H2O2 via a previously unidentified mechanism involving H2O2-activated heme transfer to apoCta1
      Title: Respiration triggers heme transfer from cytochrome c peroxidase to catalase in yeast mitochondria.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    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 catalase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables catalase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables catalase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables catalase activity IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    enables catalase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables heme binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables heme binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables peroxidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in cellular oxidant detoxification IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in hydrogen peroxide catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in hydrogen peroxide catabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in hydrogen peroxide catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in hydrogen peroxide catabolic process IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in hydrogen peroxide catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in response to hydrogen peroxide IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in response to oxidative stress IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in response to reactive oxygen species IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in mitochondrial matrix IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in mitochondrion IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in peroxisomal matrix IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in peroxisomal matrix IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in peroxisome IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in peroxisome IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    catalase A
    NP_010542.1
    • Catalase A; breaks down hydrogen peroxide in the peroxisomal matrix formed by acyl-CoA oxidase (Pox1p) during fatty acid beta-oxidation

    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_001136.10 Reference assembly

      Range
      968133..969680 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180564.1 → NP_010542.1  TPA: catalase A [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010542.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VSN6, E9P947, P15202
      UniProtKB/TrEMBL
      A0A6A5PZS8, A6ZYK8, B3LG34, C7GTJ1, C8Z5G8, G2WAZ9, N1P8H9
      Conserved Domains (1) summary
      cd08157
      Location:47 → 502
      catalase_fungal; Fungal catalases similar to yeast catalases A and T
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P15202.1

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