| IED ID | IndEnz0018001698 |
| Enzyme Type ID | peroxidase001698 |
| Protein Name |
Peroxiredoxin DOT5 Prx EC 1.11.1.24 Disrupter of telomere silencing protein 5 Nuclear thiol peroxidase nTPx Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin DOT5 |
| Gene Name | DOT5 YIL010W |
| 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 | MGEALRRSTRIAISKRMLEEEESKLAPISTPEVPKKKIKTGPKHNANQAVVQEANRSSDVNELEIGDPIPDLSLLNEDNDSISLKKITENNRVVVFFVYPRASTPGCTRQACGFRDNYQELKKYAAVFGLSADSVTSQKKFQSKQNLPYHLLSDPKREFIGLLGAKKTPLSGSIRSHFIFVDGKLKFKRVKISPEVSVNDAKKEVLEVAEKFKEE |
| Enzyme Length | 215 |
| Uniprot Accession Number | P40553 |
| Absorption | |
| Active Site | ACT_SITE 107; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000269|PubMed:12730197 |
| 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:10681558, ECO:0000269|PubMed:12730197}; |
| DNA Binding | |
| EC Number | 1.11.1.24 |
| Enzyme Function | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Has a role in telomere silencing, which is the repression of chromatin structure which leads to a stop in the transcription of nearby genes. Also has a role in the regulation of telomere length. Acts as an alkyl-hydroperoxide reductase in the nucleus during post-diauxic growth. Preferentially reduces alkyl-hydroperoxides rather than hydrogen peroxide. Acts as an antioxidant necessary for stationary phase survival. {ECO:0000269|PubMed:12730197, ECO:0000269|PubMed:12925864, ECO:0000269|PubMed:9755194}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:10681558}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (9); Chain (1); Compositional bias (1); Disulfide bond (1); Domain (1); Helix (5); Mutagenesis (2); Region (1); Turn (1) |
| Keywords | 3D-structure;Antioxidant;Chromosome;Disulfide bond;Nucleus;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome;Telomere;Transcription;Transcription regulation |
| Interact With | |
| Induction | INDUCTION: During the diauxic shift. In response to oxidative stress. {ECO:0000269|PubMed:12730197}. |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:12925864, ECO:0000269|PubMed:14562095}. Chromosome, telomere {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2A4V; |
| Mapped Pubmed ID | 11283351; 14690591; 15051715; 18021067; 18084888; 19424433; 19536198; 19538506; 19543365; 21282621; 22094416; 22209905; 22970195; 2408019; 25173844; 26685013; 26740819; |
| Motif | |
| Gene Encoded By | |
| Mass | 24,120 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |