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 24-JUN-2015, entry version 93. 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; Cyanobacteria; Oscillatoriophycideae; Chroococcales; 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., RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the RT entire genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [2] RP SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME 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) RT reduce unsaturated fatty acid hydroperoxides in Synechocystis PCC RT 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 RT in Synechocystis PCC 6803 during the progression of oxidative RT stress."; RL Plant Physiol. 136:2855-2861(2004). CC -!- FUNCTION: Hydroperoxy fatty acid reductase essential for the CC removal of lipid hydroperoxides under normal and stress CC conditions, leading to the protection of membrane integrity. CC {ECO:0000269|PubMed:15347790}. CC -!- CATALYTIC ACTIVITY: A hydroperoxy fatty acid + NADPH = a hydroxy CC fatty acid + NADP(+) + H(2)O. {ECO:0000269|PubMed:11418106}. CC -!- ENZYME REGULATION: Mercaptosuccinate, pCMB, and nethylmaleimide CC act as inhibitors of the catalytic activity. CC {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 CC salt 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 RefSeq; YP_005651722.1; NC_017277.1. DR RefSeq; YP_007451546.1; NC_020286.1. DR ProteinModelPortal; P74250; -. DR STRING; 1148.SYNGTS_1769; -. DR PeroxiBase; 3755; SYspGPx01. DR PaxDb; P74250; -. DR EnsemblBacteria; BAA18344; BAA18344; BAA18344. DR KEGG; syn:slr1171; -. DR PATRIC; 23840787; VBISynSp132158_1948. DR eggNOG; COG0386; -. DR InParanoid; P74250; -. DR KO; K00432; -. DR OMA; MSTEIYA; -. DR OrthoDB; EOG66QM2H; -. 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:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR029759; GPX_AS. DR InterPro; IPR029760; GPX_CS. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR11592; PTHR11592; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 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 Complete proteome; NADP; Oxidoreductase; Peroxidase; KW Reference proteome. FT CHAIN 1 169 Hydroperoxy fatty acid reductase gpx1. FT /FTId=PRO_0000066663. FT ACT_SITE 41 41 {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 //