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   03-AUG-2022, entry version 123.
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; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified 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}.
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DR   EMBL; BA000022; BAA18344.1; -; Genomic_DNA.
DR   PIR; S75885; S75885.
DR   AlphaFoldDB; P74250; -.
DR   SMR; P74250; -.
DR   STRING; 1148.1653430; -.
DR   PeroxiBase; 3755; SYspGPx01.
DR   PaxDb; P74250; -.
DR   EnsemblBacteria; BAA18344; BAA18344; BAA18344.
DR   KEGG; syn:slr1171; -.
DR   eggNOG; COG0386; Bacteria.
DR   InParanoid; P74250; -.
DR   OMA; FPMMSKI; -.
DR   PhylomeDB; P74250; -.
DR   BioCyc; MetaCyc:MON-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   CDD; cd00340; GSH_Peroxidase; 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; 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   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