ID A0A0F2NWL6_9FLAO Unreviewed; 183 AA.
AC A0A0F2NWL6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=VR77_05465 {ECO:0000313|EMBL:KJS06444.1};
OS Flavobacteriales bacterium BRH_c54.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX NCBI_TaxID=1629721 {ECO:0000313|EMBL:KJS06444.1, ECO:0000313|Proteomes:UP000033681};
RN [1] {ECO:0000313|EMBL:KJS06444.1, ECO:0000313|Proteomes:UP000033681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c54 {ECO:0000313|EMBL:KJS06444.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-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:KJS06444.1}.
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DR EMBL; LADZ01000021; KJS06444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2NWL6; -.
DR STRING; 1629721.VR77_05465; -.
DR PATRIC; fig|1629721.3.peg.836; -.
DR Proteomes; UP000033681; 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 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.
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}.
FT ACT_SITE 61
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 183 AA; 20758 MW; 2D3F3E81D9286A0D CRC64;
MKKISFMILL LGLFSGFNSK VTPEEKKNLY HLSFTDINGK EVNMKDFKGK NIVIVNVASE
CGFTTQYEDL QKLHEAYKEN TVVIGFPCNQ FGGQEPGSEE EIATFCKKNF GVTFLLASKI
DVKGENTHPI YQWLTAKSEN GVMDSSVKWN FQKYVINKQG ELVDVFYSVT NPMSDKITKL
LKD
//
