| IED ID | IndEnz0018001485 |
| Enzyme Type ID | peroxidase001485 |
| Protein Name |
Peroxiredoxin-5, mitochondrial EC 1.11.1.24 Peroxiredoxin V Prx-V Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin 5 |
| Gene Name | PRDX5 |
| Organism | Papio hamadryas (Hamadryas baboon) |
| 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 Cercopithecoidea Cercopithecidae (Old World monkeys) Cercopithecinae Papio (baboons) Papio hamadryas (Hamadryas baboon) |
| Enzyme Sequence | MGLAGVCVLRRSAGYILGGAAGQSVAATAAARRRSEGGWASGGVRSFSRAAAAMAPIKVGDAIPAVEVFEGEPGNKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAEALKAKGVQVLACLSVNDAFVTGEWGRAHKVEGKVRLLADPTGAFGKETDLLLDDSLVSIFGNRRLKRFSMVVQDGIVKALNVEPDGTGLTCSLAPSIISQL |
| Enzyme Length | 215 |
| Uniprot Accession Number | Q9GLW9 |
| Absorption | |
| Active Site | ACT_SITE 101; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:P30044 |
| 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:P30044}; |
| 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. {ECO:0000250|UniProtKB:P30044}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Chain (1); Disulfide bond (1); Domain (1); Lipidation (1); Modified residue (6); Motif (1); Transit peptide (1) |
| Keywords | Acetylation;Alternative initiation;Antioxidant;Cytoplasm;Disulfide bond;Lipoprotein;Mitochondrion;Oxidoreductase;Palmitate;Peroxidase;Peroxisome;Phosphoprotein;Redox-active center;Transit peptide |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000250|UniProtKB:P30044}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic+peroxisomal]: Cytoplasm {ECO:0000250|UniProtKB:P30044}. Peroxisome matrix {ECO:0000250|UniProtKB:P30044}. |
| Modified Residue | MOD_RES 76; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P99029; MOD_RES 84; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P30044; MOD_RES 84; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P99029; MOD_RES 117; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P99029; MOD_RES 172; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9R063; MOD_RES 183; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P99029 |
| Post Translational Modification | PTM: S-palmitoylated. Palmitoylation occurs on the active site, inhibiting its reactivity; therefore PRDX5 palmitoylation status determines its antioxidant capacity. {ECO:0000250|UniProtKB:P30044}.; PTM: [Isoform Mitochondrial]: S-palmitoylated. Depalmitoylated by ABHD10. {ECO:0000250|UniProtKB:P30044}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 213..215; /note=Microbody targeting signal; /evidence=ECO:0000250|UniProtKB:P30044 |
| Gene Encoded By | |
| Mass | 22,166 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |