GPX2_SYNY3
ID GPX2_SYNY3 Reviewed; 154 AA.
AC P73824;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Hydroperoxy fatty acid reductase Gpx2;
DE EC=1.11.1.22;
GN Name=gpx2; OrderedLocusNames=slr1992;
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 PROTEIN SEQUENCE OF 1-16.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
RN [4]
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=57.3 uM for NADPH {ECO:0000269|PubMed:11418106};
CC KM=82.1 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, and salt stress conditions
CC increase the expression level. {ECO:0000269|PubMed:15347790}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; BA000022; BAA17881.1; -; Genomic_DNA.
DR PIR; S75019; S75019.
DR AlphaFoldDB; P73824; -.
DR SMR; P73824; -.
DR IntAct; P73824; 8.
DR STRING; 1148.1652964; -.
DR PaxDb; P73824; -.
DR EnsemblBacteria; BAA17881; BAA17881; BAA17881.
DR KEGG; syn:slr1992; -.
DR eggNOG; COG0386; Bacteria.
DR InParanoid; P73824; -.
DR OMA; LAPFKGQ; -.
DR PhylomeDB; P73824; -.
DR BioCyc; MetaCyc:MON-17843; -.
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; IPR036249; Thioredoxin-like_sf.
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; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NADP; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298645"
FT CHAIN 2..154
FT /note="Hydroperoxy fatty acid reductase Gpx2"
FT /id="PRO_0000424245"
FT ACT_SITE 34
FT /evidence="ECO:0000250"
FT CONFLICT 6
FT /note="S -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="P -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 16646 MW; 3758EF5DF85DEEB2 CRC64;
MPLPTSLTTL DGTPLAPEVI ADKVVLFVNV ASKCGLTPQY SGLVALDKAY GEKGLVIIGV
PCNQFGAQEP GSPEEIKDFT KTKYDVDFTL LEKQDVNGPN RSPLYQFLVG DGEDISWNFG
KFLIGRDGQV VARFDPQTKP DDTNLKAAIE KALG
