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Database: UniProt
Entry: A0A133Y1S4_9BACT
LinkDB: A0A133Y1S4_9BACT
Original site: A0A133Y1S4_9BACT 
ID   A0A133Y1S4_9BACT        Unreviewed;       184 AA.
AC   A0A133Y1S4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=HMPREF1870_02442 {ECO:0000313|EMBL:KXB37134.1};
OS   Bacteroidales bacterium KA00344.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1497954 {ECO:0000313|EMBL:KXB37134.1, ECO:0000313|Proteomes:UP000070254};
RN   [1] {ECO:0000313|Proteomes:UP000070254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA00344 {ECO:0000313|Proteomes:UP000070254};
RA   Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA   O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA   Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-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:KXB37134.1}.
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DR   EMBL; LSCT01000213; KXB37134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133Y1S4; -.
DR   STRING; 1497954.HMPREF1870_02442; -.
DR   PATRIC; fig|1497954.3.peg.2498; -.
DR   OrthoDB; 9789406at2; -.
DR   Proteomes; UP000070254; 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; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070254}.
FT   ACT_SITE        36
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   184 AA;  21205 MW;  7538B5A775575065 CRC64;
     MRTVYEFSVK DRKGKDVSLK EYANEVLLIV NTATKCGFTP TYTELENTFQ KYHAQGFEIL
     DFPCNQFGQQ APGTDASIHK FCKLTYGTDF PRFKKIKVNG DDADPLYKFL KKQKGFAGWD
     ESHELFPVLD KMLSEADPNY KDSADIKWNF TKFLINKKGQ VVKRYEPTEK IDNICADIET
     LLAE
//
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