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Database: UniProt
Entry: A0A150WKB0_BDEBC
LinkDB: A0A150WKB0_BDEBC
Original site: A0A150WKB0_BDEBC 
ID   A0A150WKB0_BDEBC        Unreviewed;       174 AA.
AC   A0A150WKB0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=AZI86_14385 {ECO:0000313|EMBL:KYG64152.1};
OS   Bdellovibrio bacteriovorus.
OC   Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC   Pseudobdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=959 {ECO:0000313|EMBL:KYG64152.1, ECO:0000313|Proteomes:UP000075320};
RN   [1] {ECO:0000313|EMBL:KYG64152.1, ECO:0000313|Proteomes:UP000075320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R0 {ECO:0000313|EMBL:KYG64152.1,
RC   ECO:0000313|Proteomes:UP000075320};
RA   Ploux O.;
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:KYG64152.1}.
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DR   EMBL; LUKE01000003; KYG64152.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150WKB0; -.
DR   Proteomes; UP000075320; 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   Reference proteome {ECO:0000313|Proteomes:UP000075320}.
FT   DOMAIN          9..171
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   174 AA;  19554 MW;  971BE8AEC041B05F CRC64;
     MSTFAASPTS APDLFYELSA QDINGRKVNF STYRGKVVLV VNTASECGFT PQLAELEALY
     KKHANQGFVV LAFPSNDFKQ EKADNKEIQA FATKEYHTTF PFFEKAPVRG DDKQPVYQFL
     TEKKPGILFK DVGWNFEKFL INRKGEVVDR WSSITKPSSG SITKAIEKAL SEPL
//
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