ID A0A1I6ZJ54_9ACTN Unreviewed; 164 AA.
AC A0A1I6ZJ54;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=SAMN05660657_02012 {ECO:0000313|EMBL:SFT62687.1};
OS Geodermatophilus amargosae.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1296565 {ECO:0000313|EMBL:SFT62687.1, ECO:0000313|Proteomes:UP000199546};
RN [1] {ECO:0000313|Proteomes:UP000199546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46136 {ECO:0000313|Proteomes:UP000199546};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPBA01000005; SFT62687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6ZJ54; -.
DR STRING; 1296565.SAMN05660657_02012; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000199546; 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; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
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; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 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 DOMAIN 1..163
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 37
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 164 AA; 17284 MW; 29A83D36A03D9D11 CRC64;
MTDLLDLPVS TLQGEDTTLG ALTGGGPALV VNVASRCGLT PQYTQLEELQ REYGPRGFTV
VGVPCNQFAG QEPGTAEEIA GFCSATYGVT FPMTGKVEVN GDGAHPVYQR LTEAPDAAGE
SGPVQWNFEK FLVDADGAVV ARFRPMTDPG APEVRTAIEA LLPR
//