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Database: UniProt
Entry: A0A168QZ28_9BACL
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Original site: A0A168QZ28_9BACL 
ID   A0A168QZ28_9BACL        Unreviewed;       159 AA.
AC   A0A168QZ28;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=PBAT_01710 {ECO:0000313|EMBL:OAB48379.1};
OS   Paenibacillus antarcticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=253703 {ECO:0000313|EMBL:OAB48379.1, ECO:0000313|Proteomes:UP000077355};
RN   [1] {ECO:0000313|EMBL:OAB48379.1, ECO:0000313|Proteomes:UP000077355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5836 {ECO:0000313|EMBL:OAB48379.1,
RC   ECO:0000313|Proteomes:UP000077355};
RA   Shin S.-K., Yi H.;
RT   "Draft genome sequence of Paenibacillus antarcticus CECT 5836.";
RL   Submitted (MAR-2016) 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:OAB48379.1}.
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DR   EMBL; LVJI01000001; OAB48379.1; -; Genomic_DNA.
DR   RefSeq; WP_068646012.1; NZ_LVJI01000001.1.
DR   AlphaFoldDB; A0A168QZ28; -.
DR   OrthoDB; 9789406at2; -.
DR   Proteomes; UP000077355; 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; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF78; PHOSPHOLIPID HYDROPEROXIDE 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; PS00763; GLUTATHIONE_PEROXID_2; 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   Reference proteome {ECO:0000313|Proteomes:UP000077355}.
FT   DOMAIN          1..159
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   159 AA;  18011 MW;  E405D382B2A5D22B CRC64;
     MSIYNYQVNT IRGEQVSLSD YQGKVLLIVN TASKCGFTPQ YTGLQELYEK FKDHNFEILG
     FPSNQFKEQE PGSSEDIEQF CQINHGVTFP LFEKIDVKGN TAHPLFQYLS KQAPGVLGST
     AVKWNFTKFL VDSDGKVIQR FAPATTPDKL EHIIDDLLK
//
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