| IED ID | IndEnz0018000393 |
| Enzyme Type ID | peroxidase000393 |
| Protein Name |
Thioredoxin-dependent peroxide reductase, mitochondrial EC 1.11.1.24 PRx III Peroxiredoxin-3 PRX-3 Thioredoxin-dependent peroxiredoxin 3 |
| Gene Name | Prdx3 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MAAAAGRLLWSSVARPASTIFRSISASTVLRPVASRRTCLTDMLWSACPQAKFAFSTSSSFHTPAVTQHAPHFKGTAVVNGEFKELSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLGHMNITLLSDLTKQISRDYGVLLESAGIALRGLFIIDPNGVIKHLSVNDLPVGRSVEEPLRLVKAFQFVETHGEVCPANWTPESPTIKPSPTASKEYFEKVHQ |
| Enzyme Length | 257 |
| Uniprot Accession Number | Q9Z0V6 |
| Absorption | |
| Active Site | ACT_SITE 109; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:P35705 |
| 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:0000250|UniProtKB:P30048}; |
| 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. {ECO:0000250|UniProtKB:P30048}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Domain (1); Modified residue (4); Sequence conflict (2); Transit peptide (1) |
| Keywords | Acetylation;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Endosome;Lipoprotein;Mitochondrion;Oxidoreductase;Palmitate;Peroxidase;Phosphoprotein;Redox-active center;Reference proteome;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P35705}. Cytoplasm {ECO:0000250|UniProtKB:P30048}. Early endosome {ECO:0000250|UniProtKB:P30048}. Note=Localizes to early endosomes in a RPS6KC1-dependent manner. {ECO:0000250|UniProtKB:P30048}. |
| Modified Residue | MOD_RES 84; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P20108; MOD_RES 92; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P30048; MOD_RES 92; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P20108; MOD_RES 147; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P30048 |
| Post Translational Modification | PTM: Phosphorylated by LRRK2; phosphorylation reduces perodixase activity. {ECO:0000250|UniProtKB:P30048}.; PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) and sulphonic acid (C(P)-SO3H) instead of its condensation to a disulfide bond. {ECO:0000250|UniProtKB:P30048}.; PTM: S-palmitoylated. {ECO:0000250|UniProtKB:P20108}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12887684; 16396496; 16518874; 19935650; 27523322; |
| Motif | |
| Gene Encoded By | |
| Mass | 28,295 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |