ID   GPX_ENCCU               Reviewed;         177 AA.
AC   Q8SSH7;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Probable phospholipid hydroperoxide glutathione peroxidase;
DE            Short=PHGPx;
DE            EC=1.11.1.12;
GN   OrderedLocusNames=ECU02_0440;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL
RP   STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
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   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AL590442; CAD25075.1; -; Genomic_DNA.
DR   RefSeq; NP_584571.1; NM_001040760.1.
DR   AlphaFoldDB; Q8SSH7; -.
DR   SMR; Q8SSH7; -.
DR   STRING; 284813.Q8SSH7; -.
DR   PeroxiBase; 5976; EcuGPx01.
DR   PRIDE; Q8SSH7; -.
DR   GeneID; 858561; -.
DR   KEGG; ecu:ECU02_0440; -.
DR   VEuPathDB; MicrosporidiaDB:ECU02_0440; -.
DR   HOGENOM; CLU_029507_0_1_1; -.
DR   InParanoid; Q8SSH7; -.
DR   OMA; LAPFKGQ; -.
DR   OrthoDB; 1483113at2759; -.
DR   Proteomes; UP000000819; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; 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; 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; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Oxidoreductase; Peroxidase; Reference proteome; Stress response.
FT   CHAIN           1..177
FT                   /note="Probable phospholipid hydroperoxide glutathione
FT                   peroxidase"
FT                   /id="PRO_0000383333"
FT   ACT_SITE        42
FT                   /evidence="ECO:0000250|UniProtKB:P36968"
SQ   SEQUENCE   177 AA;  20029 MW;  8003A8F26D94F578 CRC64;
     MERGMESEAF YGLSARGWDG SEVSLGSFRG CVIMIANVAS SCKFAESNYK SFAGLLDKFY
     RKGLRILLFP CNQYLGQESR PIEEIRGEVS KKYSDRFVVF DKVDVFGKGA HPVFRHLVNT
     KNGKGRLGNF IKWNFTKFLV DRKGCVVKRF GPSDIVKEDD ENLLRSIEDG ENGMQNS