ID Q7VYL8_BORPE Unreviewed; 233 AA.
AC Q7VYL8;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Glutathione transferase {ECO:0000313|EMBL:CAE41596.1};
DE EC=2.5.1.18 {ECO:0000313|EMBL:CAE41596.1};
GN OrderedLocusNames=BP1300 {ECO:0000313|EMBL:CAE41596.1};
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE41596.1, ECO:0000313|Proteomes:UP000002676};
RN [1] {ECO:0000313|Proteomes:UP000002676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC {ECO:0000313|Proteomes:UP000002676};
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|RuleBase:RU003494}.
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DR EMBL; BX640414; CAE41596.1; -; Genomic_DNA.
DR RefSeq; NP_880067.1; NC_002929.2.
DR RefSeq; WP_010930296.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VYL8; -.
DR STRING; 257313.BP1300; -.
DR PaxDb; 257313-BP1300; -.
DR GeneID; 69601217; -.
DR KEGG; bpe:BP1300; -.
DR PATRIC; fig|257313.5.peg.1401; -.
DR eggNOG; COG0625; Bacteria.
DR HOGENOM; CLU_011226_14_4_4; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR CDD; cd10291; GST_C_YfcG_like; 1.
DR CDD; cd03048; GST_N_Ure2p_like; 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; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44051:SF19; DISULFIDE-BOND OXIDOREDUCTASE YFCG; 1.
DR PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01151; Main.2:_Nu-like; 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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002676};
KW Transferase {ECO:0000313|EMBL:CAE41596.1}.
FT DOMAIN 1..87
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 90..212
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 233 AA; 26429 MW; 9B91D0D13DAFFF00 CRC64;
MIDLYYWTTP NGHKITLFLE ETGLPYRIHP VNISKGEQFQ PEFLAIAPNN RIPAIVDQAP
ADGGTPIPLF ESGAILLYLA EKTGQFIPAD LRGRADVLQW LFWQMGGLGP MAGQNHHFSA
YAPERIPYAI ERYVKETNRL YGVLDRQLAQ REFVAGDYSI ADMAAYPWIV PHERQGQDLN
EFPNLKRWFE AIGARPATQR AYALADRINT KPSVDTEESR RVLFGQTAAN VRR
//
