ID M1MJ14_9CLOT Unreviewed; 157 AA.
AC M1MJ14;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN Name=gpo {ECO:0000313|EMBL:AGF54831.1};
GN ORFNames=Cspa_c10550 {ECO:0000313|EMBL:AGF54831.1};
OS Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF54831.1, ECO:0000313|Proteomes:UP000011728};
RN [1] {ECO:0000313|EMBL:AGF54831.1, ECO:0000313|Proteomes:UP000011728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium saccharoperbutylacetonicum N1-4(HMT).";
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}.
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DR EMBL; CP004121; AGF54831.1; -; Genomic_DNA.
DR RefSeq; WP_015391156.1; NZ_AOIF01000140.1.
DR AlphaFoldDB; M1MJ14; -.
DR STRING; 36745.CLSAP_10600; -.
DR KEGG; csr:Cspa_c10550; -.
DR PATRIC; fig|931276.5.peg.1011; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_4_0_9; -.
DR OrthoDB; 9809733at2; -.
DR Proteomes; UP000011728; 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 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 InterPro; IPR013766; Thioredoxin_domain.
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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011728}.
FT DOMAIN 1..157
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 35
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 157 AA; 18118 MW; E29F6BCD43F8899D CRC64;
MNFYDFAANK MNGKEIKMEE YKGKVILIVN TASKCGLTPQ LEGLENLYKE YKDKNFEILG
FPCNQFANQD PGTNKEISEF CLINYGVTFM MFEKIDVNGQ KAHPIYKFLK ENAKGTFGSE
IKWNFTKFLI DKEGNVIKRY APITTPEKIK SDIEKLL
//
