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AHP1 thioredoxin peroxidase AHP1 [ Saccharomyces cerevisiae S288C ]

Gene ID: 850799, updated on 3-Nov-2024

Summary

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Official Symbol
AHP1
Official Full Name
thioredoxin peroxidase AHP1
Primary source
SGD:S000004099
Locus tag
YLR109W
See related
AllianceGenome:SGD:S000004099; FungiDB:YLR109W; VEuPathDB:YLR109W
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 thioredoxin peroxidase activity. Involved in cell redox homeostasis; cellular response to oxidative stress; and response to metal ion. Located in cytoplasm. Orthologous to human PRDX5 (peroxiredoxin 5). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See AHP1 in Genome Data Viewer
Location:
chromosome: XII
Exon count:
1
Sequence:
Chromosome: XII; NC_001144.5 (368781..369311)

Chromosome XII - NC_001144.5Genomic Context describing neighboring genes Neighboring gene ncRNA Neighboring gene uncharacterized protein Neighboring gene Ccw12p Neighboring gene uncharacterized protein

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. Identification in Saccharomyces cerevisiae of a new stable variant of alkyl hydroperoxide reductase 1 (Ahp1) induced by oxidative stress. Prouzet-Mauléon V, et al. J Biol Chem, 2002 Feb 15. PMID 11719517
  2. In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. Verdoucq L, et al. J Biol Chem, 1999 Jul 9. PMID 10391912
  3. Alkyl hydroperoxide reductase 1 protects Saccharomyces cerevisiae against metal ion toxicity and glutathione depletion. Nguyên-nhu NT, et al. Toxicol Lett, 2002 Oct 5. PMID 12270680
  4. Characterization of the yeast peroxiredoxin Ahp1 in its reduced active and overoxidized inactive forms using NMR. Trivelli X, et al. Biochemistry, 2003 Dec 9. PMID 14640681
  5. 1H, 13C and 15N backbone resonance assignments of the dimeric yeast peroxiredoxin YLR109w. Trivelli X, et al. J Biomol NMR, 2004 Jan. PMID 14739647

See all (104) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Redox requirements for ubiquitin-like urmylation of Ahp1, a 2-Cys peroxiredoxin from yeast.
    Title: Redox requirements for ubiquitin-like urmylation of Ahp1, a 2-Cys peroxiredoxin from yeast.
  2. The results point to the stress-related proteins Ahp1, Yhb1 and Oye2, as well as Gln1 and Kes1 as putative candidates for being evaluated as biomarkers for diagnostic assays of S. cerevisiae infections.
    Title: Immunoproteomic profiling of Saccharomyces cerevisiae systemic infection in a murine model.
  3. Its overexpression results in a reduced ROS level and fails to reverse saccharomyces cerevisiae gorowth defect in the stationary phase.
    Title: Requirement of peroxiredoxin on the stationary phase of yeast cell growth.
  4. The structure of the Ahp1-Trx2 complex showed for the first time how the electron transfers from thioredoxin to a peroxidase with a thioredoxin-like fold.
    Title: Structural snapshots of yeast alkyl hydroperoxide reductase Ahp1 peroxiredoxin reveal a novel two-cysteine mechanism of electron transfer to eliminate reactive oxygen species.
Submit: New GeneRIF Correction

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 peroxidase activity IEA
Inferred from Electronic Annotation
more info
  
enables thioredoxin peroxidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables thioredoxin peroxidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables thioredoxin peroxidase activity IEA
Inferred from Electronic Annotation
more info
  
enables thioredoxin peroxidase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables thioredoxin-dependent peroxiredoxin activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in cell redox homeostasis IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in cell redox homeostasis IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in cell redox homeostasis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in cellular oxidant detoxification IEA
Inferred from Electronic Annotation
more info
  
involved_in cellular response to oxidative stress IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in cellular response to oxidative stress IEA
Inferred from Electronic Annotation
more info
  
involved_in cellular response to oxidative stress IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in hydrogen peroxide catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in response to metal ion 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 cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol HDA PubMed 
is_active_in mitochondrion IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in peroxisome IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in plasma membrane HDA PubMed 

General protein information

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Preferred Names
thioredoxin peroxidase AHP1
NP_013210.1
  • Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p

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
    368781..369311
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001181996.1 → NP_013210.1  TPA: thioredoxin peroxidase AHP1 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_013210.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VYA9, P38013
    UniProtKB/TrEMBL
    A7A113, B3LT76, B5VN47, C7GQT1, C8ZD80, G2WIV3, N1NZ91
    Conserved Domains (1) summary
    COG0678
    Location:1 → 176
    AHP1; Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P38013.4

Gene LinkOut

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