| IED ID | IndEnz0018001259 |
| Enzyme Type ID | peroxidase001259 |
| Protein Name |
Peroxiredoxin-1 EC 1.11.1.24 Macrophage 23 kDa stress protein Osteoblast-specific factor 3 OSF-3 Thioredoxin peroxidase 2 Thioredoxin-dependent peroxide reductase 2 Thioredoxin-dependent peroxiredoxin 1 |
| Gene Name | Prdx1 Msp23 Paga Tdpx2 |
| 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 | MSSGNAKIGYPAPNFKATAVMPDGQFKDISLSEYKGKYVVFFFYPLDFTFVCPTEIIAFSDRADEFKKLNCQVIGASVDSHFCHLAWINTPKKQGGLGPMNIPLISDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITINDLPVGRSVDEIIRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVNKSKEYFSKQK |
| Enzyme Length | 199 |
| Uniprot Accession Number | P35700 |
| Absorption | |
| Active Site | ACT_SITE 52; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:Q06830 |
| 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 (PubMed:19766572). {ECO:0000250|UniProtKB:Q06830, ECO:0000269|PubMed:19766572}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Cross-link (3); Disulfide bond (2); Domain (1); Initiator methionine (1); Modified residue (9); Sequence conflict (1) |
| Keywords | Acetylation;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Isopeptide bond;Oxidoreductase;Peroxidase;Phosphoprotein;Redox-active center;Reference proteome;Ubl conjugation |
| Interact With | Itself; Q13043 |
| Induction | INDUCTION: By oxidative and sulfhydryl-reactive agents. |
| 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:0007744|PubMed:23806337; MOD_RES 90; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q06830; MOD_RES 136; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:23806337 |
| 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 | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10501973; 10632718; 11217851; 11741941; 12466851; 12519079; 12520002; 12627171; 12891360; 12904583; 14610273; 14681479; 15161859; 15448164; 15627969; 15741177; 15858817; 16170382; 16297875; 16615898; 16635246; 16880205; 17408621; 17634366; 17640558; 17697936; 17921138; 18544346; 18614015; 18689572; 18799693; 19098005; 19369943; 19455133; 19521566; 19647805; 19941984; 20018613; 20178744; 20683885; 20697350; 21239607; 21319188; 21516123; 21565611; 21677750; 22099303; 23101509; 23186333; 23237955; 23375831; 23421996; 23487789; 23602274; 23624931; 23909438; 24715692; 25975898; 26496610; 26726832; 27434733; 27517622; 27605010; 27689697; 27926878; 28485790; 28605287; 28659575; 28893373; 29901182; 30097850; 30111318; 30185517; 30696882; 30991142; 31026770; 31028193; 31419957; 31526567; 32682987; 32705184; 32736685; 33254076; 9371744; 9507200; |
| Motif | |
| Gene Encoded By | |
| Mass | 22,176 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |