| IED ID | IndEnz0018000878 |
| Enzyme Type ID | peroxidase000878 |
| Protein Name |
Peroxiredoxin-5, mitochondrial EC 1.11.1.24 Antioxidant enzyme B166 AOEB166 Liver tissue 2D-page spot 2D-0014IV PLP Peroxiredoxin V Prx-V Peroxisomal antioxidant enzyme Thioredoxin peroxidase PMP20 Thioredoxin-dependent peroxiredoxin 5 |
| Gene Name | Prdx5 Prdx6 |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MLQLGLRVLGCKASSVLRASTCLAGRAGRKEAGWECGGARSFSSSAVTMAPIKVGDAIPSVEVFEGEPGKKVNLAELFKGKKGVLFGVPGAFTPGCSKTHLPGFVEQAGALKAKGAQVVACLSVNDVFVIEEWGRAHQAEGKVRLLADPTGAFGKATDLLLDDSLVSLFGNRRLKRFSMVIDNGIVKALNVEPDGTGLTCSLAPNILSQL |
| Enzyme Length | 210 |
| Uniprot Accession Number | P99029 |
| Absorption | |
| Active Site | ACT_SITE 96; /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:0000269|PubMed:10679306}; |
| 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:0000269|PubMed:10679306}. |
| 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 (8); Motif (1); Sequence conflict (2); Transit peptide (1) |
| Keywords | Acetylation;Alternative initiation;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Lipoprotein;Mitochondrion;Oxidoreductase;Palmitate;Peroxidase;Peroxisome;Phosphoprotein;Redox-active center;Reference proteome;Transit peptide |
| Interact With | P08228 |
| 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 70; /note=N6-acetyllysine; alternate; /evidence=ECO:0007744|PubMed:23576753; MOD_RES 70; /note=N6-succinyllysine; alternate; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 71; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:23576753; MOD_RES 79; /note=N6-acetyllysine; alternate; /evidence=ECO:0007744|PubMed:23576753; MOD_RES 79; /note=N6-succinyllysine; alternate; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 112; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 167; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9R063; MOD_RES 178; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079 |
| Post Translational Modification | PTM: S-palmitoylated. Palmitoylation occurs on the active site, inhibiting its reactivity; therefore PRDX5 palmitoylation status determines its antioxidant capacity. {ECO:0000269|PubMed:31740833}.; PTM: [Isoform Mitochondrial]: S-palmitoylated. Depalmitoylated by ABHD10. {ECO:0000250|UniProtKB:P30044}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10501973; 10751410; 11217851; 11278957; 12466851; 12654475; 12805289; 14610273; 14651853; 15618518; 15858817; 16602821; 16615898; 18614015; 19098005; 19834914; 20345759; 21267068; 21677750; 22988430; 23461683; 23831231; 23909438; 24044889; 25975898; 27121020; 27689697; 27786251; 29128334; 29620243; 29777756; 30044981; 30097850; 31196623; 31217524; 31358548; 31505325; 32205843; 32643149; 32824836; 34637923; 34888938; 35132351; |
| Motif | MOTIF 208..210; /note=Microbody targeting signal; /evidence=ECO:0000250|UniProtKB:P30044 |
| Gene Encoded By | |
| Mass | 21,897 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |