ID   A0A258P7S5_9BURK        Unreviewed;       198 AA.
AC   A0A258P7S5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=B7Y60_04430 {ECO:0000313|EMBL:OYY38490.1};
OS   Polaromonas sp. 35-63-35.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1970418 {ECO:0000313|EMBL:OYY38490.1, ECO:0000313|Proteomes:UP000216365};
RN   [1] {ECO:0000313|EMBL:OYY38490.1, ECO:0000313|Proteomes:UP000216365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35-63-35 {ECO:0000313|EMBL:OYY38490.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) 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:OYY38490.1}.
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DR   EMBL; NCFQ01000003; OYY38490.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A258P7S5; -.
DR   Proteomes; UP000216365; 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:SF44; GLUTATHIONE PEROXIDASE; 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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..198
FT                   /note="Glutathione peroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012129940"
FT   DOMAIN          21..197
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        76
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   198 AA;  21804 MW;  993CB6148B9E234C CRC64;
     MKHPSFNPWP MWALLAAMAA LTPARAAPPG AGAAQEAPAC APLLQHSFLR LQDEKPQSLC
     QYSGKVLVVV NTASFCGFTR QYAGLEALYA RYRDQGLVVL GFPSNDFSQE SGSNKEIADF
     CENTFGVKFP MFVKSGVTGK TANPLFRQLA DKTGQRPRWN FHKYVVARDG QRVTSFNTAT
     DPKDPAFLKD IEEKLLGK
//