ID   Q2KZ75_BORA1            Unreviewed;       202 AA.
AC   Q2KZ75;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Glutathione transferase {ECO:0000313|EMBL:CAJ49753.1};
GN   OrderedLocusNames=BAV2143 {ECO:0000313|EMBL:CAJ49753.1};
OS   Bordetella avium (strain 197N).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ49753.1, ECO:0000313|Proteomes:UP000001977};
RN   [1] {ECO:0000313|EMBL:CAJ49753.1, ECO:0000313|Proteomes:UP000001977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N {ECO:0000313|EMBL:CAJ49753.1,
RC   ECO:0000313|Proteomes:UP000001977};
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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DR   EMBL; AM167904; CAJ49753.1; -; Genomic_DNA.
DR   RefSeq; WP_012417808.1; NC_010645.1.
DR   AlphaFoldDB; Q2KZ75; -.
DR   STRING; 360910.BAV2143; -.
DR   GeneID; 41393982; -.
DR   KEGG; bav:BAV2143; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_12_2_4; -.
DR   OrthoDB; 8634103at2; -.
DR   Proteomes; UP000001977; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd03205; GST_C_6; 1.
DR   CDD; cd03049; GST_N_3; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1.
DR   PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW   Transferase {ECO:0000313|EMBL:CAJ49753.1}.
FT   DOMAIN          1..78
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          83..202
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   202 AA;  22595 MW;  402E5DD82E060C5F CRC64;
     MKLIGSLTSP YVRKVRVVMA EKKLDYQLEL ENVWSPDTKI QQFNPLGKIP CLVMEDGGAL
     FDSRVIVEYL DTLSPVARLI PQSGRERAAV KSWEAIADGV LDACLAIVKE KQRAEDRRSP
     EWIERQYGKI HAALRAMDGS LGDNVHCMGV NYTLADIAVG CALGYLDLRF ADLNWRADHP
     NLTRLHDKLS LRASFAETKP TG
//