ID A0A5M9DSU1_WEIPA Unreviewed; 156 AA. AC A0A5M9DSU1; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 17-JUN-2020, entry version 3. DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499}; GN ORFNames=FKV73_03925 {ECO:0000313|EMBL:KAA8438271.1}; OS Weissella paramesenteroides (Leuconostoc paramesenteroides). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae; OC Weissella. OX NCBI_TaxID=1249 {ECO:0000313|EMBL:KAA8438271.1, ECO:0000313|Proteomes:UP000324493}; RN [1] {ECO:0000313|EMBL:KAA8438271.1, ECO:0000313|Proteomes:UP000324493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DmW_118 {ECO:0000313|EMBL:KAA8438271.1, RC ECO:0000313|Proteomes:UP000324493}; RX PubMed=31527278; DOI=.1073/pnas.1907787116; RA Rudman S.M., Greenblum S., Hughes R.C., Rajpurohit S., Kiratli O., RA Lowder D.B., Lemmon S.G., Petrov D.A., Chaston J.M., Schmidt P.; RT "Microbiome composition shapes rapid genomic adaptation of Drosophila RT melanogaster."; RL Proc. Natl. Acad. Sci. U.S.A. 116:20025-20032(2019). CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC {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:KAA8438271.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; VHPB01000006; KAA8438271.1; -; Genomic_DNA. DR Proteomes; UP000324493; 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; -; 1. DR InterPro; IPR000889; Glutathione_peroxidase. DR InterPro; IPR029759; GPX_AS. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11592; PTHR11592; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. DR PRINTS; PR01011; GLUTPROXDASE. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1. PE 3: Inferred from homology; KW Oxidoreductase {ECO:0000256|RuleBase:RU000499}; KW Peroxidase {ECO:0000256|RuleBase:RU000499, ECO:0000313|EMBL:KAA8438271.1}. FT ACT_SITE 36 FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1" SQ SEQUENCE 156 AA; 17690 MW; 187BE9FE69A3342F CRC64; MTTIYDFTET EMNGKPINLK DYEGKVVIIV NTASKCGLAP QLEGLEALYK EHKDEGLVVL GLPSNQFKQE LDSDEETNEF CQMHYGVTFP MTKRVMVNGQ DEDELFTYLK EQSGNGAIKW NYTKFLVGRD GKLIHRYAPI TTPEKMTDDV LAALKD //