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Database: UniProt
Entry: A0A0T6UYG7_9PSED
LinkDB: A0A0T6UYG7_9PSED
Original site: A0A0T6UYG7_9PSED 
ID   A0A0T6UYG7_9PSED        Unreviewed;       160 AA.
AC   A0A0T6UYG7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=AO726_04280 {ECO:0000313|EMBL:KRW62642.1};
OS   Pseudomonas sp. TTU2014-080ASC.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1729724 {ECO:0000313|EMBL:KRW62642.1, ECO:0000313|Proteomes:UP000051864};
RN   [1] {ECO:0000313|EMBL:KRW62642.1, ECO:0000313|Proteomes:UP000051864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTU2014-080ASC {ECO:0000313|EMBL:KRW62642.1,
RC   ECO:0000313|Proteomes:UP000051864};
RA   Webb H.E., Bugarel M., Den Bakker H.C., Nightingale K., Granier S.A.,
RA   Loneragan G.H.;
RT   "Carbapenem-non-susceptible Bacteria Recovered from the Faeces of Dairy
RT   Cattle.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRW62642.1}.
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DR   EMBL; LKKK01000001; KRW62642.1; -; Genomic_DNA.
DR   RefSeq; WP_058066796.1; NZ_LKKK01000001.1.
DR   AlphaFoldDB; A0A0T6UYG7; -.
DR   STRING; 1729724.AO726_04280; -.
DR   OrthoDB; 9785502at2; -.
DR   Proteomes; UP000051864; 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   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.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051864}.
FT   ACT_SITE        36
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   160 AA;  17668 MW;  FB4238733A6A3A6A CRC64;
     MSAFHDLSLR ALDGQELPLA PYKDQLVLVV NVASKCGLTP QYAALEKLYQ QYKNRGFTVL
     GLPCNQFAGQ EPDSEEAIRE FCTLNYGVTF PLGSKLEVNG PDRHPLYRLL AGEGAEFPGD
     ITWNFEKFLV GHDGRVLARF SPRTSPDDPA VIQAIEKALG
//
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