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Database: UniProt
Entry: A0A0R2T771_9FLAO
LinkDB: A0A0R2T771_9FLAO
Original site: A0A0R2T771_9FLAO 
ID   A0A0R2T771_9FLAO        Unreviewed;       191 AA.
AC   A0A0R2T771;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=ABR87_07155 {ECO:0000313|EMBL:KRO82870.1};
OS   Cryomorphaceae bacterium BACL7 MAG-121220-bin83.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX   NCBI_TaxID=1655595 {ECO:0000313|EMBL:KRO82870.1, ECO:0000313|Proteomes:UP000051535};
RN   [1] {ECO:0000313|EMBL:KRO82870.1, ECO:0000313|Proteomes:UP000051535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL29 MAG-121220-bin83 {ECO:0000313|EMBL:KRO82870.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-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:KRO82870.1}.
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DR   EMBL; LICF01000017; KRO82870.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2T771; -.
DR   Proteomes; UP000051535; 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   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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..191
FT                   /note="Glutathione peroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006424460"
SQ   SEQUENCE   191 AA;  21223 MW;  C793492104CE075A CRC64;
     MKKLSSLLRM SLIGMLVGCG QTVAQPVSGP VDFYSLSANT LEGEAFSFEQ LRGKRVLIVN
     TASECGFTPQ YKDLQALWEM TDHASFVILG FPCNDFGNQE SGTADEIQSF CSKSYGVTFQ
     MMEKVSIKGV NPHPVYQWLT QKEQNGNSDA HVRWNFCKFA VNEMGQWNAS YLMTTSPLSK
     DIKSFAGVTK D
//
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