ID   GPX4_TOBAC              Reviewed;         169 AA.
AC   Q9FXS3;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Probable phospholipid hydroperoxide glutathione peroxidase;
DE            Short=PHGPx;
DE            EC=1.11.1.12;
DE   AltName: Full=Nt-SubC08;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Takemoto D., Kawakita K.;
RT   "Molecular cloning of elicitor inducible genes of tobacco.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By fungal elicitor.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AB041518; BAB16430.1; -; mRNA.
DR   AlphaFoldDB; Q9FXS3; -.
DR   SMR; Q9FXS3; -.
DR   STRING; 4097.Q9FXS3; -.
DR   PeroxiBase; 2869; NtGPx06-1A.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
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   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   2: Evidence at transcript level;
KW   Cytoplasm; Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..169
FT                   /note="Probable phospholipid hydroperoxide glutathione
FT                   peroxidase"
FT                   /id="PRO_0000066636"
FT   ACT_SITE        43
FT                   /evidence="ECO:0000250|UniProtKB:P36968"
SQ   SEQUENCE   169 AA;  18785 MW;  E01918069ED98A71 CRC64;
     MASQSSKPQS IYDFTVKDAK GNDVDLSIYK GKVLIIVNVA SQCGLTNSNY TDMTEIYKKY
     KDQGLEILAF PCNQFGGQEP GSIEEIQNMV CTRFKAEYPI FDKVDVNGDN AAPLYKFLKS
     SKGGFFGDSI KWNFSKFLVD KEGNVVDRYS PTTTPASMEK DIKKLLGVA