ID A0A1M3G017_9SPHI Unreviewed; 197 AA.
AC A0A1M3G017;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=BGO54_19200 {ECO:0000313|EMBL:OJW32513.1};
OS Sphingobacteriales bacterium 46-32.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895839 {ECO:0000313|EMBL:OJW32513.1, ECO:0000313|Proteomes:UP000184358};
RN [1] {ECO:0000313|EMBL:OJW32513.1, ECO:0000313|Proteomes:UP000184358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=46-32 {ECO:0000313|EMBL:OJW32513.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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:OJW32513.1}.
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DR EMBL; MKTY01000020; OJW32513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3G017; -.
DR STRING; 1895839.BGO54_19200; -.
DR Proteomes; UP000184358; 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 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; 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 74
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 197 AA; 22019 MW; 7F7C5EC0B434958D CRC64;
MTIRQRIMKT IYPVIMWVSK LTGGRARALA DGNEKTQPLQ SIYDLHVTLN NGKDLDLASL
KGKKILIVNT ASNCGYTHQY EALQELSAKY NHQLEVIGFP ANDFKEQEKG SDEEIASFCK
VNYGVTFPLA RKSTVVPGAE QHPVFYWLTH AAANGWNNQA PVWNFSKYLI AEDGRLLGYF
DPGVSPLAEA ITNQLDK
//
