ID A0A1I2U9R6_9SPHI Unreviewed; 168 AA.
AC A0A1I2U9R6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=SAMN04489864_10245 {ECO:0000313|EMBL:SFG73838.1};
OS Pedobacter insulae.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=414048 {ECO:0000313|EMBL:SFG73838.1, ECO:0000313|Proteomes:UP000199666};
RN [1] {ECO:0000313|EMBL:SFG73838.1, ECO:0000313|Proteomes:UP000199666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18684 {ECO:0000313|EMBL:SFG73838.1,
RC ECO:0000313|Proteomes:UP000199666};
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; FOPP01000002; SFG73838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2U9R6; -.
DR STRING; 414048.SAMN04489864_10245; -.
DR OrthoDB; 9789406at2; -.
DR Proteomes; UP000199666; 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: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.
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:UP000199666}.
FT DOMAIN 1..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 168 AA; 19172 MW; D4839BE36DB7EA11 CRC64;
MDFTQTIYPF KVKFLNGKEQ NLAAYANKVL LVVNTASGCG FTPQLKELQD LRSEYANEGF
EILGFPSNDF GSQEPLDGSK LNEFCEVNYG VQFPVFEKVM VRGDAAHPLF KFLRSKKLNG
HLNSTPKWNF HKYLINRKGE VVDFFYSFTK PSSSKVKKKI QRLLAEGK
//
