IED ID | IndEnz0018000003 |
Enzyme Type ID | peroxidase000003 |
Protein Name |
Glutathione peroxidase-like peroxiredoxin HYR1 EC 1.11.1.24 Glutathione peroxidase homolog 3 GPx 3 Hydrogen peroxide resistance protein 1 Oxidant receptor peroxidase 1 Phospholipid hydroperoxide glutathione peroxidase 3 PHGPx3 |
Gene Name | HYR1 GPX3 ORP1 YIR037W |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Enzyme Sequence | MSEFYKLAPVDKKGQPFPFDQLKGKVVLIVNVASKCGFTPQYKELEALYKRYKDEGFTIIGFPCNQFGHQEPGSDEEIAQFCQLNYGVTFPIMKKIDVNGGNEDPVYKFLKSQKSGMLGLRGIKWNFEKFLVDKKGKVYERYSSLTKPSSLSETIEELLKEVE |
Enzyme Length | 163 |
Uniprot Accession Number | P40581 |
Absorption | |
Active Site | ACT_SITE 36; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000269|PubMed:17720812, ECO:0000305|PubMed:18767166" |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000269|PubMed:12437921, ECO:0000269|PubMed:18767166}; |
DNA Binding | |
EC Number | 1.11.1.24 |
Enzyme Function | FUNCTION: Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator YAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging, being the most active of three closely related S.cerevisiae peroxiredoxins (GPX1, GPX2, and HYR1/GPX3) with respect to peroxide and lipid hydroperoxide reduction. The three enzymes are not required for the glutaredoxin-mediated antioxidant function. In the presence of peroxides, HYR1/GPX3 is directly oxidized at Cys-36 to form a cysteine sulfenic acid (-SOH). Cys-36-SOH then forms either an intramolecular disulfide bond (Cys-36 with Cys-82) or a transient, intermolecular disulfide bond with 'Cys-598' of YAP1, which is further resolved into a YAP1 intramolecular disulfide bond ('Cys-303' with 'Cys-598'), which causes its nuclear accumulation and activation, and a reduced Cys-36 in HYR1/GPX3. {ECO:0000269|PubMed:10480913, ECO:0000269|PubMed:11445588, ECO:0000269|PubMed:12437921, ECO:0000269|PubMed:12743123, ECO:0000269|PubMed:14556853, ECO:0000269|PubMed:15337745, ECO:0000269|PubMed:17720812, ECO:0000269|PubMed:19230722, ECO:0000269|PubMed:9315326}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Beta strand (7); Chain (1); Disulfide bond (2); Helix (7); Mutagenesis (1) |
Keywords | 3D-structure;Antioxidant;Cytoplasm;Disulfide bond;Mitochondrion;Oxidoreductase;Peroxidase;Peroxisome;Redox-active center;Reference proteome |
Interact With | |
Induction | INDUCTION: In contrast to the other two peroxiredoxins, HYR1/GPX3 expression is constitutive, not stress-induced. {ECO:0000269|PubMed:10480913}. |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}. Peroxisome matrix {ECO:0000269|PubMed:22659048}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 3CMI; |
Mapped Pubmed ID | 10688190; 11018134; 11283351; 12464172; 12702279; 14616057; 14690591; 15133656; 15706081; 15953550; 16251355; 16554755; 16677071; 16754991; 16790465; 16808898; 17505968; 17561102; 17707771; 18021067; 18039473; 18084898; 18178164; 18199679; 18270585; 18309271; 18385160; 18467557; 18719252; 19140447; 19376195; 19424433; 19538123; 19715675; 19755417; 20145245; 20370606; 20538604; 20626317; 20959147; 21036150; 21072575; 21229313; 21229323; 21282621; 21310260; 21734149; 21844193; 21912624; 21918511; 21933953; 22094416; 22209905; 22685415; 22970195; 23198979; 23974869; 24074273; 24410772; 24563858; 25173844; 25218923; 26261310; 26813659; 27089838; 27373166; |
Motif | |
Gene Encoded By | |
Mass | 18,641 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:62620 |
Cross Reference Brenda |