ID A0A1F9WET6_9BACT Unreviewed; 167 AA.
AC A0A1F9WET6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 28-JUN-2023, entry version 14.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=A3J70_14245 {ECO:0000313|EMBL:OGS13667.1};
OS Elusimicrobia bacterium RIFCSPHIGHO2_02_FULL_61_10.
OC Bacteria; Elusimicrobiota.
OX NCBI_TaxID=1797944 {ECO:0000313|EMBL:OGS13667.1, ECO:0000313|Proteomes:UP000176716};
RN [1] {ECO:0000313|EMBL:OGS13667.1, ECO:0000313|Proteomes:UP000176716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGS13667.1}.
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DR EMBL; MGUP01000572; OGS13667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F9WET6; -.
DR Proteomes; UP000176716; 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 37
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 167 AA; 17957 MW; DFA5DB15AED37EF4 CRC64;
MEKTIYDLKV KDAHGEAYSL AGLKGKVILI VNVASKCGFT PQYEGLEALH KKYGEKGLAV
LGFPCNQFGG QEPGSNEEIQ HFCKLTYGAS FPVLGKLEVN GPGADPLYVY LKEKAPGVLG
SEAIKWNFTK FLVDRTGKVA GRYAPATKPE ALAPDIEKAL ALSPSKP
//
