ID   GPX1_PEA                Reviewed;         236 AA.
AC   O24296;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Phospholipid hydroperoxide glutathione peroxidase, chloroplastic;
DE            Short=PHGPx;
DE            EC=1.11.1.12;
DE   Flags: Precursor;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Birte;
RX   PubMed=9680987; DOI=10.1046/j.1365-313x.1998.00052.x;
RA   Mullineaux P.M., Karpinski S., Jimenez A., Cleary S.P., Robinson C.,
RA   Creissen G.P.;
RT   "Identification of cDNAS encoding plastid-targeted glutathione
RT   peroxidase.";
RL   Plant J. 13:375-379(1998).
CC   -!- FUNCTION: Protects cells and enzymes from oxidative damage, by
CC       catalyzing the reduction of hydrogen peroxide, lipid peroxides and
CC       organic hydroperoxide, by glutathione. {ECO:0000250|UniProtKB:O70325}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a
CC         hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O;
CC         Xref=Rhea:RHEA:19057, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:58297, ChEBI:CHEBI:131871, ChEBI:CHEBI:134019;
CC         EC=1.11.1.12; Evidence={ECO:0000250|UniProtKB:P36968};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ000508; CAA04142.1; -; mRNA.
DR   PIR; T06462; T06462.
DR   AlphaFoldDB; O24296; -.
DR   SMR; O24296; -.
DR   PeroxiBase; 2897; PsGPx01.
DR   EnsemblPlants; Psat6g026280.1; Psat6g026280.1.cds; Psat6g026280.
DR   Gramene; Psat6g026280.1; Psat6g026280.1.cds; Psat6g026280.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; IEA:UniProtKB-EC.
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   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   2: Evidence at transcript level;
KW   Chloroplast; Oxidoreductase; Peroxidase; Plastid; Transit peptide.
FT   TRANSIT         1..64
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           65..236
FT                   /note="Phospholipid hydroperoxide glutathione peroxidase,
FT                   chloroplastic"
FT                   /id="PRO_0000013087"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000250|UniProtKB:P36968"
SQ   SEQUENCE   236 AA;  26400 MW;  85300731A3455E5D CRC64;
     MASMAFSTTF FTPLRDFNQP RTNSTPSTSL PFTKSSIASS KSPFFQLGFS QQASSNFPIV
     PSKTRSFSVN AKAIKDKTIY DFTVKDIDKK DVSLSKFKGK VLLIVNVASR CGLTSSNYTE
     LSHLYENFKN KGLEVLAFPC NQFGMQEPGS NEEIKQFACT KFKAEFPIFD KVDVNGPFTA
     PVYQFLKSSS GGFFGDIVKW NFEKFLVDKN GKVVERYPPT TSPFQIEKDI QKLLAA