ID   A0A1I6KVY5_9BURK        Unreviewed;       206 AA.
AC   A0A1I6KVY5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=SAMN05428960_3967 {ECO:0000313|EMBL:SFR95178.1};
OS   Mitsuaria sp. PDC51.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=1881035 {ECO:0000313|EMBL:SFR95178.1, ECO:0000313|Proteomes:UP000199246};
RN   [1] {ECO:0000313|EMBL:SFR95178.1, ECO:0000313|Proteomes:UP000199246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PDC51 {ECO:0000313|EMBL:SFR95178.1,
RC   ECO:0000313|Proteomes:UP000199246};
RA   de Groot N.N.;
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; FOZE01000002; SFR95178.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6KVY5; -.
DR   STRING; 1881035.SAMN05428960_3967; -.
DR   OrthoDB; 9785502at2; -.
DR   Proteomes; UP000199246; 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; IPR006311; TAT_signal.
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; PS51318; TAT; 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:UP000199246};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..206
FT                   /note="Glutathione peroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011757065"
FT   DOMAIN          23..203
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   206 AA;  22000 MW;  28844B620375526D CRC64;
     MNTSFGSLLR RAAFAGLAMV AMALATTAAH AAPAAEPATS GAACPELLNR QMPRLQDEKP
     QALCQYAGKV VLVVNTASFC GYTPQYKALE AVSARYADKG LVVLGFPSGD FGNQEYGSNK
     EIAEFCENTF NVKFPMFSKS SVAAGKADLN PLFADLAKRT GQAPKWNFHK YLISRDGKQV
     MSFASGVSPD SSTFTQAVEK LLAQPQ
//