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Database: UniProt
Entry: A0A0L0KI24_9ACTN
LinkDB: A0A0L0KI24_9ACTN
Original site: A0A0L0KI24_9ACTN 
ID   A0A0L0KI24_9ACTN        Unreviewed;       162 AA.
AC   A0A0L0KI24;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=IQ63_09770 {ECO:0000313|EMBL:KND37209.1};
OS   Streptomyces acidiscabies.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=42234 {ECO:0000313|EMBL:KND37209.1, ECO:0000313|Proteomes:UP000037151};
RN   [1] {ECO:0000313|Proteomes:UP000037151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA   Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT   "Genome sequencing of plant-pathogenic Streptomyces species.";
RL   Submitted (JUL-2014) 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:KND37209.1}.
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DR   EMBL; JPPY01000068; KND37209.1; -; Genomic_DNA.
DR   RefSeq; WP_050370283.1; NZ_KQ257813.1.
DR   AlphaFoldDB; A0A0L0KI24; -.
DR   PATRIC; fig|42234.21.peg.2014; -.
DR   OrthoDB; 9785502at2; -.
DR   Proteomes; UP000037151; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037151}.
FT   ACT_SITE        35
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   162 AA;  17831 MW;  130242DD78A7C48A CRC64;
     MSLYDIPVRT LAGEPGDLSP YRGKVLLVVN VASRCGRTPQ YAALEEVHRR YGPRGFTVLG
     FPCNQFGQQE PGTSEEIQEF CSATYDVTFP LFEKVDVNGA RQHPVYEILT AAHDEHGVGG
     DIEWNFEKFL VSADGAVIQR IGSRVKPDAP DVIARIEALL PA
//
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