| IED ID | IndEnz0018000858 |
| Enzyme Type ID | peroxidase000858 |
| Protein Name |
Peroxiredoxin-1 EC 1.11.1.24 Natural killer cell-enhancing factor A NKEF-A Proliferation-associated gene protein PAG Thioredoxin peroxidase 2 Thioredoxin-dependent peroxide reductase 2 Thioredoxin-dependent peroxiredoxin 1 |
| Gene Name | PRDX1 PAGA PAGB TDPX2 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVQKSKEYFSKQK |
| Enzyme Length | 199 |
| Uniprot Accession Number | Q06830 |
| Absorption | |
| Active Site | ACT_SITE 52; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000305|PubMed:12059788, ECO:0000305|PubMed:12161445" |
| 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:11986303, ECO:0000269|PubMed:9497357}; |
| 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) (PubMed:9497357). 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:0000269|PubMed:9497357}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (10); Chain (1); Compositional bias (1); Cross-link (3); Disulfide bond (2); Domain (1); Helix (9); Initiator methionine (1); Modified residue (9); Mutagenesis (2); Natural variant (1); Region (1); Sequence conflict (4); 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 | P10275; Q86TI2-2; Q8N7X4; P04156; P60484; Q9BYN0; Q13043; P54274; P13693 |
| Induction | INDUCTION: Constitutively expressed in most human cells; is induced to higher levels upon serum stimulation in untransformed and transformed cells. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:9497357}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. |
| Modified Residue | MOD_RES 2; /note="N-acetylserine"; /evidence="ECO:0007744|PubMed:25944712"; MOD_RES 7; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 16; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 27; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 32; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 35; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 35; /note="N6-succinyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P35700"; MOD_RES 90; /note="Phosphothreonine; by CDK1"; /evidence="ECO:0000269|PubMed:11986303"; 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 more than 80% decrease in enzymatic activity. {ECO:0000269|PubMed:11986303}.; PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner. {ECO:0000269|PubMed:12059788, ECO:0000269|PubMed:12161445, ECO:0000269|PubMed:12714748, ECO:0000269|PubMed:12853451, ECO:0000269|PubMed:18172504, ECO:0000269|PubMed:19812042}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 2RII; 3HY2; 4XCS; 7LJ1; |
| Mapped Pubmed ID | 10514471; 10821856; 11771746; 11904290; 12080185; 12506115; 12577067; 12650976; 12714747; 14703116; 14743216; 15161933; 15448164; 15590625; 15864612; 15890005; 15955662; 16169070; 16189514; 16278420; 16677601; 16990800; 17176052; 17234762; 17352427; 17519234; 17540176; 17557078; 17601350; 17603937; 17606720; 17707450; 17761673; 17786348; 17909037; 18281480; 18344994; 18501712; 18549262; 18606987; 18624398; 18691386; 18977241; 18992915; 19016754; 19113821; 19119138; 19135121; 19156129; 19167051; 19286652; 19298244; 19338310; 19367725; 19369943; 19406930; 19558833; 19737972; 19738201; 19766572; 19805454; 19822145; 19834914; 19902980; 20029029; 20178744; 20237496; 20381070; 20562859; 20589759; 20610706; 20631257; 20647304; 20711500; 20877624; 21044950; 21159870; 21273562; 21343392; 21385867; 21401077; 21516123; 21565611; 21988832; 22158042; 22215146; 22236188; 22323290; 22446018; 22475482; 22492841; 22537621; 22623428; 22810585; 22877757; 22902630; 22985558; 23060010; 23065574; 23113308; 23241402; 23277276; 23334324; 23386615; 23421996; 23479738; 23615915; 23723070; 23737084; 23914992; 24009050; 24062305; 24152995; 24189400; 24297309; 24316730; 24412244; 24480440; 25011585; 25082442; 25162226; 25426613; 25484280; 25579166; 25609649; 26117319; 26150388; 26159854; 26170166; 26301632; 26478675; 26496610; 26548861; 26617696; 26636537; 26689287; 26752685; 27142532; 27177495; 27388124; 27503926; 27517622; 27612662; 27653015; 27756681; 27924073; 28009281; 28082197; 28219939; 28314261; 28348082; 28398822; 29063384; 29302025; 29582423; 29656298; 29673884; 29687844; 29773556; 29884768; 29908016; 30284335; 30287919; 30567989; 30693924; 30862546; 30886505; 30981892; 31158443; 31366734; 31429766; 31470801; 31477836; 31580947; 31613423; 31901729; 32284348; 32357862; 32736685; 32739204; 33011678; 33147465; 33338736; 33712558; 33747258; 34055579; 34208049; 34260286; 34322898; 34389806; 34409853; |
| Motif | |
| Gene Encoded By | |
| Mass | 22,110 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda | 1.11.1.24; |