ID E0SGY3_DICD3 Unreviewed; 183 AA.
AC E0SGY3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Thioredoxin/glutathione peroxidase BtuE {ECO:0000256|HAMAP-Rule:MF_02061};
DE EC=1.11.1.24 {ECO:0000256|HAMAP-Rule:MF_02061};
DE EC=1.11.1.9 {ECO:0000256|HAMAP-Rule:MF_02061};
GN Name=btuE {ECO:0000256|HAMAP-Rule:MF_02061,
GN ECO:0000313|EMBL:ADM98961.1};
GN OrderedLocusNames=Dda3937_03647 {ECO:0000313|EMBL:ADM98961.1};
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADM98961.1, ECO:0000313|Proteomes:UP000006859};
RN [1] {ECO:0000313|EMBL:ADM98961.1, ECO:0000313|Proteomes:UP000006859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937 {ECO:0000313|EMBL:ADM98961.1,
RC ECO:0000313|Proteomes:UP000006859};
RX PubMed=21217001; DOI=10.1128/JB.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
CC -!- FUNCTION: Non-specific peroxidase that can use thioredoxin or
CC glutathione as a reducing agent. {ECO:0000256|HAMAP-Rule:MF_02061}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02061};
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. BtuE
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02061}.
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DR EMBL; CP002038; ADM98961.1; -; Genomic_DNA.
DR RefSeq; WP_013318404.1; NC_014500.1.
DR AlphaFoldDB; E0SGY3; -.
DR STRING; 198628.Dda3937_03647; -.
DR GeneID; 9734201; -.
DR KEGG; ddd:Dda3937_03647; -.
DR PATRIC; fig|198628.6.peg.2753; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_1_2_6; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
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 HAMAP; MF_02061; Thiored_glutath_peroxid; 1.
DR InterPro; IPR033674; BtuE.
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, ECO:0000256|HAMAP-
KW Rule:MF_02061};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_02061}; Reference proteome {ECO:0000313|Proteomes:UP000006859}.
FT ACT_SITE 37
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02061,
FT ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 183 AA; 20455 MW; 1BDCCDD898ABC2B6 CRC64;
MSNTLYAIPL QTIDGRQASL ENWRNNVLLV VNVASQCGLT KQYEALENLY ETYRDRGFAV
LGFPSNEFAG QEPGSNEEIN AFCRGTFGVQ FPMFGKINVN GSGRHPLYQA LIQAQPEALR
PQGSEFYERR VSKGQAPAHP GDILWNFEKF LVNRRSEVIA RFSPDMTPDD GAIIKAIEQA
LAQ
//
