| IED ID | IndEnz0018001660 |
| Enzyme Type ID | peroxidase001660 |
| Protein Name |
Peroxiredoxin tpx1 EC 1.11.1.24 Thioredoxin peroxidase TPx Thioredoxin-dependent peroxiredoxin tpx1 |
| Gene Name | tpx1 tsa1 SPCC576.03c |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MSLQIGKPAPDFKGTAVVNGAFEEIKLADYKGKWVFLGFYPLDFTFVCPTEIVAFSEAASKFAERNAQVILTSTDSEYSHLAFINTPRKEGGLGGINIPLLADPSHKVSRDYGVLIEDAGVAFRGLFLIDPKGVLRQITINDLPVGRSVDEALRLLDAFQFVEEHGEVCPANWHKGSDTIDTKNPEKYFSKH |
| Enzyme Length | 192 |
| Uniprot Accession Number | O74887 |
| Absorption | |
| Active Site | ACT_SITE 48; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000305|PubMed:24316080 |
| 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:20356456}; |
| 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 (PubMed:17409354, PubMed:20356456). Relays hydrogen peroxide as a signal to the transcription factor pap1 by inducing the formation of intramolecular disulfide bonds in pap1, which causes its nuclear accumulation and activation (PubMed:15824112, PubMed:24316080). Reduced by srx1 and this regulation acts as a molecular switch controlling the transcriptional response to hydrogen peroxide (PubMed:15956211). {ECO:0000269|PubMed:15824112, ECO:0000269|PubMed:15956211, ECO:0000269|PubMed:17409354, ECO:0000269|PubMed:20356456, ECO:0000269|PubMed:24316080}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Modified residue (2); Mutagenesis (5) |
| Keywords | Antioxidant;Cytoplasm;Disulfide bond;Nucleus;Oxidoreductase;Peroxidase;Phosphoprotein;Redox-active center;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:24316080}. Nucleus {ECO:0000269|PubMed:16823372}. |
| Modified Residue | MOD_RES 105; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18257517; MOD_RES 148; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:18257517 |
| Post Translational Modification | PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin srx1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner. {ECO:0000269|PubMed:15824112, ECO:0000269|PubMed:15956211}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19547744; 19682301; 20473289; 22245228; 23697806; 24268782; 24521463; 25720772; 26412298; 26537787; 29996109; 30726745; 33823663; |
| Motif | |
| Gene Encoded By | |
| Mass | 21,191 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda | 1.11.1.24; |