Detail Information for IndEnz0018000876
IED ID IndEnz0018000876
Enzyme Type ID peroxidase000876
Protein Name Peroxiredoxin-5, mitochondrial
EC 1.11.1.24
Peroxiredoxin V
Prx-V
Thioredoxin peroxidase
Thioredoxin-dependent peroxiredoxin 5
Fragment
Gene Name PRDX5
Organism Mesocricetus auratus (Golden hamster)
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 Cricetidae Cricetinae (hamsters) Mesocricetus Mesocricetus auratus (Golden hamster)
Enzyme Sequence ETDLLLDDSLVSLFGNRR
Enzyme Length 18
Uniprot Accession Number P86241
Absorption
Active Site
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 Chain (1); Domain (1); Modified residue (1); Non-terminal residue (2)
Keywords Antioxidant;Cytoplasm;Mitochondrion;Oxidoreductase;Peroxidase;Peroxisome;Phosphoprotein;Redox-active center;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P30044}. Cytoplasm {ECO:0000250|UniProtKB:P30044}. Peroxisome matrix {ECO:0000250|UniProtKB:P30044}.
Modified Residue MOD_RES 12; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9R063
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 2,063
Kinetics
Metal Binding
Rhea ID RHEA:62620
Cross Reference Brenda