ID GPX1_SYNY3 Reviewed; 169 AA. AC P74250; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Hydroperoxy fatty acid reductase gpx1; DE EC=1.11.1.22; GN Name=gpx1; OrderedLocusNames=slr1171; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [2] RP SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY RP REGULATION. RX PubMed=11418106; DOI=10.1016/s0014-5793(01)02517-0; RA Gaber A., Tamoi M., Takeda T., Nakano Y., Shigeoka S.; RT "NADPH-dependent glutathione peroxidase-like proteins (Gpx-1, Gpx-2) reduce RT unsaturated fatty acid hydroperoxides in Synechocystis PCC 6803."; RL FEBS Lett. 499:32-36(2001). RN [3] RP INDUCTION, AND FUNCTION. RX PubMed=15347790; DOI=10.1104/pp.104.044842; RA Gaber A., Yoshimura K., Tamoi M., Takeda T., Nakano Y., Shigeoka S.; RT "Induction and functional analysis of two reduced nicotinamide adenine RT dinucleotide phosphate-dependent glutathione peroxidase-like proteins in RT Synechocystis PCC 6803 during the progression of oxidative stress."; RL Plant Physiol. 136:2855-2861(2004). CC -!- FUNCTION: Hydroperoxy fatty acid reductase essential for the removal of CC lipid hydroperoxides under normal and stress conditions, leading to the CC protection of membrane integrity. {ECO:0000269|PubMed:15347790}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a hydroperoxy polyunsaturated fatty acid + H(+) + NADPH = a CC hydroxy polyunsaturated fatty acid + H2O + NADP(+); CC Xref=Rhea:RHEA:50876, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:131871, CC ChEBI:CHEBI:134019; EC=1.11.1.22; CC Evidence={ECO:0000269|PubMed:11418106}; CC -!- ACTIVITY REGULATION: Mercaptosuccinate, pCMB, and nethylmaleimide act CC as inhibitors of the catalytic activity. {ECO:0000269|PubMed:11418106}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=83.1 uM for NADPH {ECO:0000269|PubMed:11418106}; CC KM=215 uM for alpha-linolenic acid hydroperoxide CC {ECO:0000269|PubMed:11418106}; CC pH dependence: CC Optimum pH is 8.2. {ECO:0000269|PubMed:11418106}; CC Temperature dependence: CC Optimum temperature is 37 degrees Celsius. CC {ECO:0000269|PubMed:11418106}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11418106}. CC -!- INDUCTION: High light, methylviologen, t-butyl hydroperoxide, and salt CC stress conditions increase the expression level. CC {ECO:0000269|PubMed:15347790}. CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000022; BAA18344.1; -; Genomic_DNA. DR PIR; S75885; S75885. DR AlphaFoldDB; P74250; -. DR SMR; P74250; -. DR STRING; 1148.gene:10499220; -. DR PeroxiBase; 3755; SYspGPx01. DR PaxDb; 1148-1653430; -. DR EnsemblBacteria; BAA18344; BAA18344; BAA18344. DR KEGG; syn:slr1171; -. DR eggNOG; COG0386; Bacteria. DR InParanoid; P74250; -. DR PhylomeDB; P74250; -. DR BioCyc; MetaCyc:MONOMER-17842; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro. DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central. DR CDD; cd00340; GSH_Peroxidase; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR029759; GPX_AS. DR InterPro; IPR029760; GPX_CS. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1. DR PANTHER; PTHR11592:SF78; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 1: Evidence at protein level; KW NADP; Oxidoreductase; Peroxidase; Reference proteome. FT CHAIN 1..169 FT /note="Hydroperoxy fatty acid reductase gpx1" FT /id="PRO_0000066663" FT ACT_SITE 41 FT /evidence="ECO:0000250" SQ SEQUENCE 169 AA; 18452 MW; 0DC382089FCE39E2 CRC64; MTAQANNTIY GFSANALDGS PVALRDFEGK VLLIVNTASQ CGFTPQYQGL QALYNRFGDR GFTVLGFPCN QFGQQEPGGS GEIKNFCETR YGVTFPLFEK VEVNGPNAHP LFKFLTAASP GMAIPFLGGA EDIKWNFTKF LVDRQGKVVK RYGSIAKPDE IAADIEKLL //