ID A0A1V6MU31_9ACTN Unreviewed; 167 AA.
AC A0A1V6MU31;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=BM536_015015 {ECO:0000313|EMBL:OQD55777.1};
OS Streptomyces phaeoluteigriseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=114686 {ECO:0000313|EMBL:OQD55777.1, ECO:0000313|Proteomes:UP000184286};
RN [1] {ECO:0000313|Proteomes:UP000184286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41896 {ECO:0000313|Proteomes:UP000184286};
RA Schniete J.K., Salih T., Algora Gallardo L., Martinez Fernandez S.,
RA Herron P.R.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OQD55777.1, ECO:0000313|Proteomes:UP000184286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41896 {ECO:0000313|EMBL:OQD55777.1,
RC ECO:0000313|Proteomes:UP000184286};
RA Salih T.S., Algora Gallardo L., Melo Santos T., Filgueira Martinez S.,
RA Herron P.R.;
RT "Draft genome sequence of Streptomyces phaeoluteigriseus type strain
RT DSM41896.";
RL Submitted (FEB-2017) 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:OQD55777.1}.
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DR EMBL; MPOH02000011; OQD55777.1; -; Genomic_DNA.
DR RefSeq; WP_073496612.1; NZ_MPOH02000011.1.
DR AlphaFoldDB; A0A1V6MU31; -.
DR STRING; 114686.BM536_015015; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000184286; 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:SF40; THIOREDOXIN_GLUTATHIONE PEROXIDASE BTUE; 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; 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 41
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 167 AA; 17746 MW; 05A350A42135FC40 CRC64;
MTTDAGTSPL DVEIGALKGG SADLSQYAGQ AVLIVNVASK CGLTPQYNGL ERLQERYAGR
GFTVLGVPCN QFLGQEPGSA EEIAEFCSAT YGVTFPLTEK AEVNGDGRHA LYERLVGFAD
GEGHSGDIRW NFEKFLVGRD GTVVARFSPQ TEPESAEVVA AIEKQLG
//