| IED ID | IndEnz0018001231 |
| Enzyme Type ID | peroxidase001231 |
| Protein Name |
Peroxiredoxin-5, mitochondrial EC 1.11.1.24 Peroxiredoxin V Prx-V Thioredoxin peroxidase Thioredoxin-dependent peroxiredoxin 5 |
| Gene Name | PRDX5 |
| Organism | Bos taurus (Bovine) |
| 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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MRLGWLRVLGCRPGSVVSRATIVEGASTTAAGTRGCLEGILEWTFGGVRGFRSAAVAMAPIKVGDAIPSVEVFEKEPGNKVNLAELFKGKKGVLFGLPGAFTPGCSKTHLPGFVEQADALKAKGIQVVACLTVNDVFVTEEWARAHKAEGKVRLLADPSGTFGKETDLLLDDSLLFLFGNHRLKRFSMVIEDGIVKSLNVEPDGTGLTCSLAPNILSQL |
| Enzyme Length | 219 |
| Uniprot Accession Number | Q9BGI1 |
| Absorption | |
| Active Site | ACT_SITE 105; /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 (5); Motif (1); Sequence conflict (2); Transit peptide (1) |
| Keywords | Acetylation;Alternative initiation;Antioxidant;Cytoplasm;Disulfide bond;Lipoprotein;Mitochondrion;Oxidoreductase;Palmitate;Peroxidase;Peroxisome;Phosphoprotein;Redox-active center;Reference proteome;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 80; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P99029; MOD_RES 88; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P30044; MOD_RES 88; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P99029; MOD_RES 121; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P99029; MOD_RES 187; /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 217..219; /note=Microbody targeting signal; /evidence=ECO:0000250|UniProtKB:P30044 |
| Gene Encoded By | |
| Mass | 23,253 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |