Detail Information for IndEnz0018001262
IED ID IndEnz0018001262
Enzyme Type ID peroxidase001262
Protein Name Peroxiredoxin-1
EC 1.11.1.24
HBP23
Heme-binding 23 kDa protein
Thioredoxin peroxidase 2
Thioredoxin-dependent peroxide reductase 2
Thioredoxin-dependent peroxiredoxin 1
Gene Name Prdx1 Tdpx2
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 MSSGNAKIGHPAPSFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWINTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITINDLPVGRSVDEILRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVNKSKEYFSKQK
Enzyme Length 199
Uniprot Accession Number Q63716
Absorption
Active Site ACT_SITE 52; /note=Cysteine sulfenic acid (-SOH) intermediate
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:Q06830};
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. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (By similarity). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity). {ECO:0000250|UniProtKB:P0CB50, ECO:0000250|UniProtKB:Q06830}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Beta strand (10); Chain (1); Cross-link (3); Disulfide bond (2); Domain (1); Helix (8); Initiator methionine (1); Modified residue (9); Turn (1)
Keywords 3D-structure;Acetylation;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Isopeptide bond;Oxidoreductase;Peroxidase;Phosphoprotein;Redox-active center;Reference proteome;Ubl conjugation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06830}.
Modified Residue MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0000250|UniProtKB:Q06830; MOD_RES 7; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q06830; MOD_RES 16; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q06830; MOD_RES 27; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q06830; MOD_RES 32; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q06830; MOD_RES 35; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q06830; MOD_RES 35; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P35700; MOD_RES 90; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q06830; MOD_RES 136; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P35700
Post Translational Modification PTM: Phosphorylated on Thr-90 during the M-phase, which leads to a decrease in enzymatic activity. {ECO:0000250|UniProtKB:Q06830}.
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 1QQ2; 2Z9S;
Mapped Pubmed ID 11350800; 14623930; 16396496; 16619302; 17556052; 17623297; 24687852; 7488219;
Motif
Gene Encoded By
Mass 22,109
Kinetics
Metal Binding
Rhea ID RHEA:62620
Cross Reference Brenda 1.11.1.24;