ID A0A0H4P0F6_9BACI Unreviewed; 183 AA.
AC A0A0H4P0F6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=BSM4216_1156 {ECO:0000313|EMBL:AKP46455.1};
OS Bacillus smithii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP46455.1, ECO:0000313|Proteomes:UP000036353};
RN [1] {ECO:0000313|EMBL:AKP46455.1, ECO:0000313|Proteomes:UP000036353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP46455.1,
RC ECO:0000313|Proteomes:UP000036353};
RA Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., Vriesendorp B.,
RA van de Weijer A.H.P., Schaap P.J., de Vos W.M., van der Oost J.,
RA van Kranenburg R.;
RT "Complete genome sequence of thermophilic Bacillus smithii type strain DSM
RT 4216T.";
RL Submitted (JUL-2015) 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; CP012024; AKP46455.1; -; Genomic_DNA.
DR RefSeq; WP_003353609.1; NZ_CP012024.1.
DR AlphaFoldDB; A0A0H4P0F6; -.
DR STRING; 1479.BSM4216_1156; -.
DR KEGG; bsm:BSM4216_1156; -.
DR eggNOG; COG0386; Bacteria.
DR OrthoDB; 9789406at2; -.
DR Proteomes; UP000036353; 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; 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; 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}.
FT DOMAIN 1..183
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 35
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 183 AA; 21519 MW; 1AEFF4A20DEB67A3 CRC64;
MSIYQFEVEN AYGDKVSLEE FKGKVLLVVN TASKCRFTYQ FEELQKLYEK YQKQGFEILG
FPCNQFDQQE PGTSDQAASF CQLKYGVTFP MFAKIDVNGK DAHPLFHYLK QEAPFQGFDE
SNMTEKLLKI KLANDYPEWL VGDDIKWNFT KYLINKNGQV VDRYEPWEEP VDFEQNVQKL
LEE
//
