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Database: UniProt
Entry: R2QDL3_9ENTE
LinkDB: R2QDL3_9ENTE
Original site: R2QDL3_9ENTE 
ID   R2QDL3_9ENTE            Unreviewed;       157 AA.
AC   R2QDL3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=UAW_02556 {ECO:0000313|EMBL:EOH93308.1};
OS   Enterococcus haemoperoxidus ATCC BAA-382.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1158608 {ECO:0000313|EMBL:EOH93308.1, ECO:0000313|Proteomes:UP000013858};
RN   [1] {ECO:0000313|EMBL:EOH93308.1, ECO:0000313|Proteomes:UP000013858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-382 {ECO:0000313|EMBL:EOH93308.1,
RC   ECO:0000313|Proteomes:UP000013858};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Enterococcus haemoperoxidus BAA-382.";
RL   Submitted (FEB-2013) 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:EOH93308.1}.
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DR   EMBL; AJAR01000025; EOH93308.1; -; Genomic_DNA.
DR   RefSeq; WP_010762719.1; NZ_KE136479.1.
DR   AlphaFoldDB; R2QDL3; -.
DR   STRING; 155618.RV06_GL002786; -.
DR   PATRIC; fig|1158608.3.peg.2495; -.
DR   eggNOG; COG0386; Bacteria.
DR   OrthoDB; 9789406at2; -.
DR   Proteomes; UP000013858; 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        35
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   157 AA;  17681 MW;  14D0C737578EB6EE CRC64;
     MSIYDYQVKT TNDETVSLEA YRGKVLLIVN TATGCGFTPQ YEGLENLYKK YREQGLEILD
     FPCNQFGHQA PGTDQEISDF CQLTYQTTFQ TFGKIDVNGE NADPLYDFLK GEKGGLLGGA
     IKWNFTKFLV DREGNVVKRF APTVEPEKIA GDIEKLL
//
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