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Database: UniProt
Entry: A0A1I4PTB8_9PSED
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Original site: A0A1I4PTB8_9PSED 
ID   A0A1I4PTB8_9PSED        Unreviewed;       160 AA.
AC   A0A1I4PTB8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=SAMN04487858_10268 {ECO:0000313|EMBL:SFM31008.1};
OS   Pseudomonas sp. ok602.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1761898 {ECO:0000313|EMBL:SFM31008.1, ECO:0000313|Proteomes:UP000199362};
RN   [1] {ECO:0000313|Proteomes:UP000199362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK602 {ECO:0000313|Proteomes:UP000199362};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR   EMBL; FOUL01000002; SFM31008.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4PTB8; -.
DR   STRING; 1761898.SAMN04487858_10268; -.
DR   OrthoDB; 9785502at2; -.
DR   Proteomes; UP000199362; Unassembled WGS sequence.
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   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF40; THIOREDOXIN_GLUTATHIONE PEROXIDASE BTUE; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000499};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499}.
FT   DOMAIN          1..160
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   160 AA;  17491 MW;  29664E2B389B598C CRC64;
     MSAFHDLTLK ALDGQALPLA PFNGQVVLVV NVASKCGLTP QYAALENLYQ QYKDQGFSVL
     GLPCNQFAGQ EPGSEDEIKT FCSLNYGVTF PLSSKLDVNG HDRHQLYRLL AGEGAEFPGD
     ITWNFEKFLL GKDGRVLARF SPRTAPDDPT IVQAIEKALS
//
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