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
//