ID   Q8P365_XANCP            Unreviewed;       181 AA.
AC   Q8P365;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   28-JAN-2026, entry version 128.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   Name=btuE {ECO:0000313|EMBL:AAM43429.1};
GN   OrderedLocusNames=XCC4213 {ECO:0000313|EMBL:AAM43429.1};
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Xanthomonas.
OX   NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM43429.1, ECO:0000313|Proteomes:UP000001010};
RN   [1] {ECO:0000313|EMBL:AAM43429.1, ECO:0000313|Proteomes:UP000001010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC   {ECO:0000313|Proteomes:UP000001010};
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F.,
RA   Alves L.M., do Amaral A.M., Bertolini M.C., Camargo L.E., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.,
RA   Ferreira R.C., Ferro M.I., Formighieri E.F., Franco M.C., Greggio C.C.,
RA   Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G., Lemos M.V.,
RA   Locali E.C., Machado M.A., Madeira A.M., Martinez-Rossi N.M., Martins E.C.,
RA   Meidanis J., Menck C.F., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A., Silva C., de Souza R.F., Spinola L.A., Takita M.A., Tamura R.E.,
RA   Teixeira E.C., Tezza R.I., Trindade dos Santos M., Truffi D., Tsai S.M.,
RA   White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR   EMBL; AE008922; AAM43429.1; -; Genomic_DNA.
DR   RefSeq; WP_011039274.1; NC_003902.1.
DR   AlphaFoldDB; Q8P365; -.
DR   STRING; 190485.XCC4213; -.
DR   EnsemblBacteria; AAM43429; AAM43429; XCC4213.
DR   KEGG; xcc:XCC4213; -.
DR   PATRIC; fig|190485.4.peg.4518; -.
DR   eggNOG; COG0386; Bacteria.
DR   HOGENOM; CLU_029507_1_2_6; -.
DR   OrthoDB; 9785502at2; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   FunFam; 3.40.30.10:FF:000010; Glutathione 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001010}.
FT   ACT_SITE        37
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   181 AA;  19321 MW;  1342C7779851CA13 CRC64;
     MSQSIHDIPV TDINGGATSL AAHRGKVLLV VNVASKCGLT PQYEGLEALY RDKQAQGLEV
     LGFPANDFNG QEPGSEAEIA QFCQLTYDVT FPLFSKIAVT GAEIHPLYQA LTSAQPQATG
     DGPMREKLAG YGIAANPAPG VLWNFEKFLI GRDGQVIERF APDVAADDVR LRQAVDAALA
     H
//