| IED ID | IndEnz0018001390 |
| Enzyme Type ID | peroxidase001390 |
| Protein Name |
Peroxiredoxin-6 EC 1.11.1.27 1-Cys peroxiredoxin 1-Cys PRX Acidic calcium-independent phospholipase A2 aiPLA2 EC 3.1.1.4 Glutathione-dependent peroxiredoxin Lysophosphatidylcholine acyltransferase 5 LPC acyltransferase 5 LPCAT-5 Lyso-PC acyltransferase 5 EC 2.3.1.23 Non-selenium glutathione peroxidase NSGPx |
| Gene Name | PRDX6 RCJMB04_18k11 |
| Organism | Gallus gallus (Chicken) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken) |
| Enzyme Sequence | MPGLLLGDEAPNFEADTTQGGIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFSKRNVKMIALSIDSVPDHLAWSKDINAYNGDQPVEKLPFPIIADKDRELAVKLGMLDPDERDKDGMPLTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVVDSLQLTAYKKVATPVDWKCGDSVMVVPTLPDEEAKKLFPKGVFTKDLPSGKKYLRYTPQPE |
| Enzyme Length | 224 |
| Uniprot Accession Number | Q5ZJF4 |
| Absorption | |
| Active Site | ACT_SITE 46; /note=Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity; /evidence=ECO:0000250|UniProtKB:P30041; ACT_SITE 139; /note=For phospholipase activity; /evidence=ECO:0000250|UniProtKB:O35244 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.27; Evidence={ECO:0000250|UniProtKB:P30041}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:P30041}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937, ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:58342; EC=2.3.1.23; Evidence={ECO:0000250|UniProtKB:P30041}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35983, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P30041};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984; Evidence={ECO:0000250|UniProtKB:P30041}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:P30041};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:P30041}; |
| DNA Binding | |
| EC Number | 1.11.1.27; 3.1.1.4; 2.3.1.23 |
| Enzyme Function | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (By similarity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (By similarity). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity). {ECO:0000250|UniProtKB:P30041}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Initiator methionine (1); Modified residue (2); Region (1); Site (1) |
| Keywords | Antioxidant;Cytoplasm;Hydrolase;Lipid degradation;Lipid metabolism;Lysosome;Multifunctional enzyme;Oxidoreductase;Peroxidase;Phosphoprotein;Redox-active center;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35244}. Lysosome {ECO:0000250|UniProtKB:O35244}. Note=Also found in lung secretory organelles (lamellar bodies). {ECO:0000250|UniProtKB:O35244}. |
| Modified Residue | MOD_RES 88; /note=Phosphotyrosine; /evidence=ECO:0000250; MOD_RES 176; /note=Phosphothreonine; by MAPK; /evidence=ECO:0000250|UniProtKB:O35244 |
| Post Translational Modification | PTM: Irreversibly inactivated by overoxidation of Cys-46 to sulfinic acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms upon oxidative stress. {ECO:0000250|UniProtKB:P30041}.; PTM: Phosphorylation at Thr-176 by MAP kinases increases the phospholipase activity of the enzyme (By similarity). The phosphorylated form exhibits a greater lysophosphatidylcholine acyltransferase activity compared to the non-phosphorylated form (By similarity). {ECO:0000250|UniProtKB:O35244}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 22174833; |
| Motif | |
| Gene Encoded By | |
| Mass | 24,977 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62632; RHEA:15801; RHEA:12937; RHEA:35983; RHEA:35984; RHEA:41223; RHEA:41224 |
| Cross Reference Brenda | 3.1.1.4; |