Detail Information for IndEnz0018001486
IED ID IndEnz0018001486
Enzyme Type ID peroxidase001486
Protein Name Peroxiredoxin-5, mitochondrial
EC 1.11.1.24
Antioxidant enzyme B166
AOEB166
PLP
Peroxiredoxin V
Prx-V
Peroxisomal antioxidant enzyme
Thioredoxin peroxidase PMP20
Thioredoxin-dependent peroxiredoxin 5
Gene Name Prdx5
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 MVQLRFCVLGSIAGSVLRASATWTCVAGRAGRKGAGWECGGARSFSSAAVTMAPIKVGDTIPSVEVFEGEPGKKVNLAELFKDKKGVLFGVPGAFTPGCSKTHLPGFVEQAGALKAKGAQVVACLSVNDAFVTAEWGRAHQAEGKVQLLADPTGAFGKETDLLLDDSLVSLFGNRRLKRFSMVIDKGVVKALNVEPDGTGLTCSLAPNILSQL
Enzyme Length 213
Uniprot Accession Number Q9R063
Absorption
Active Site ACT_SITE 99; /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:0000269|PubMed:10521424}.
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); Natural variant (3); 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
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 74; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P99029; MOD_RES 82; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P30044; MOD_RES 82; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P99029; MOD_RES 115; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P99029; MOD_RES 170; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 181; /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 14561759; 16396496;
Motif MOTIF 211..213; /note=Microbody targeting signal; /evidence=ECO:0000250|UniProtKB:P30044
Gene Encoded By
Mass 22,179
Kinetics
Metal Binding
Rhea ID RHEA:62620
Cross Reference Brenda