| IED ID | IndEnz0018001416 |
| Enzyme Type ID | peroxidase001416 |
| Protein Name |
Thioredoxin-dependent peroxide reductase, mitochondrial EC 1.11.1.24 Antioxidant protein 1 AOP-1 HBC189 Peroxiredoxin III Prx-III Peroxiredoxin-3 Protein MER5 homolog Thioredoxin-dependent peroxiredoxin 3 |
| Gene Name | PRDX3 AOP1 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MAAAVGRLLRASVARHVSAIPWGISATAALRPAACGRTSLTNLLCSGSSQAKLFSTSSSCHAPAVTQHAPYFKGTAVVNGEFKDLSLDDFKGKYLVLFFYPLDFTFVCPTEIVAFSDKANEFHDVNCEVVAVSVDSHFSHLAWINTPRKNGGLGHMNIALLSDLTKQISRDYGVLLEGSGLALRGLFIIDPNGVIKHLSVNDLPVGRSVEETLRLVKAFQYVETHGEVCPANWTPDSPTIKPSPAASKEYFQKVNQ |
| Enzyme Length | 256 |
| Uniprot Accession Number | P30048 |
| Absorption | |
| Active Site | ACT_SITE 108; /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:0000269|PubMed:17707404, ECO:0000269|PubMed:19462976}; |
| 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 (PubMed:7733872, PubMed:17707404). Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol (PubMed:12492477). {ECO:0000269|PubMed:12492477, ECO:0000269|PubMed:17707404, ECO:0000269|PubMed:7733872}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Beta strand (8); Chain (1); Disulfide bond (2); Domain (1); Helix (8); Modified residue (4); Mutagenesis (1); Natural variant (4); Sequence conflict (1); Transit peptide (1); Turn (2) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Endosome;Lipoprotein;Mitochondrion;Oxidoreductase;Palmitate;Peroxidase;Phosphoprotein;Redox-active center;Reference proteome;Transit peptide |
| Interact With | Q9H8Y8; Q5S007; Itself; Q15935 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P35705}. Cytoplasm {ECO:0000305|PubMed:12492477}. Early endosome {ECO:0000269|PubMed:15750338}. Note=Localizes to early endosomes in a RPS6KC1-dependent manner. {ECO:0000269|PubMed:15750338}. |
| Modified Residue | MOD_RES 83; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P20108; MOD_RES 91; /note=N6-acetyllysine; alternate; /evidence=ECO:0007744|PubMed:19608861; MOD_RES 91; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P20108; MOD_RES 146; /note=Phosphothreonine; /evidence=ECO:0000305|PubMed:21850687 |
| Post Translational Modification | PTM: Phosphorylated by LRRK2; phosphorylation reduces perodixase activity. {ECO:0000269|PubMed:21850687}.; 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:0000269|PubMed:12059788}.; PTM: S-palmitoylated. {ECO:0000250|UniProtKB:P20108}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5JCG; 5UCX; |
| Mapped Pubmed ID | 10514471; 10521424; 11518528; 15046979; 16189514; 16203048; 16385451; 17601350; 18977241; 19156129; 19738201; 19805454; 20000738; 20562859; 20711500; 21182203; 21385867; 21903422; 21988832; 22304920; 22623428; 22810585; 24459295; 25416956; 25525879; 25604459; 25609649; 26496610; 29438714; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,693 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |