(data stored in SCRATCH zone)

SWISSPROT: D6XWI2_BACIE

ID   D6XWI2_BACIE            Unreviewed;       189 AA.
AC   D6XWI2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   OrderedLocusNames=Bsel_0282 {ECO:0000313|EMBL:ADH97824.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97824.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97824.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|RuleBase:RU000499}.
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DR   EMBL; CP001791; ADH97824.1; -; Genomic_DNA.
DR   RefSeq; WP_013171253.1; NC_014219.1.
DR   STRING; 439292.Bsel_0282; -.
DR   EnsemblBacteria; ADH97824; ADH97824; Bsel_0282.
DR   KEGG; bse:Bsel_0282; -.
DR   eggNOG; ENOG4108V06; Bacteria.
DR   eggNOG; COG0386; LUCA.
DR   HOGENOM; HOG000277053; -.
DR   KO; K00432; -.
DR   OMA; LAPFKGQ; -.
DR   OrthoDB; 1635499at2; -.
DR   BioCyc; BSEL439292:G1GLR-306-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
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   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
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; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XWI2.
DR   SWISS-2DPAGE; D6XWI2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000499,
KW   ECO:0000313|EMBL:ADH97824.1};
KW   Peroxidase {ECO:0000256|RuleBase:RU000499,
KW   ECO:0000313|EMBL:ADH97824.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   ACT_SITE     35     35       {ECO:0000256|PIRSR:PIRSR000303-1}.
SQ   SEQUENCE   189 AA;  21427 MW;  FF6416D31DA5E1C9 CRC64;
     MSVYDFKVKT SSGLNAPLNR YQGKVLLIVN TATKCGFTPQ LDDLQKLQDQ YGEQGLQILG
     FPSNQFDNQE PLGDGEITEF CSLNYGVNFP LFKKIDVRGE DAHPLYQHLT KAKPFNGFDM
     DHPTAKLMVS IIESKHPEYM LDDGIKWNFT KFLIDRNGEV TARFEPTVEP FDMKADIEAL
     LQSETALNQ
//

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