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Database: UniProt
Entry: A9IM80_BORPD
LinkDB: A9IM80_BORPD
Original site: A9IM80_BORPD 
ID   A9IM80_BORPD            Unreviewed;       212 AA.
AC   A9IM80;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:CAP42676.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:CAP42676.1};
GN   OrderedLocusNames=Bpet2333 {ECO:0000313|EMBL:CAP42676.1};
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP42676.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP42676.1, ECO:0000313|Proteomes:UP000001225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC   {ECO:0000313|Proteomes:UP000001225};
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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DR   EMBL; AM902716; CAP42676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IM80; -.
DR   STRING; 94624.Bpet2333; -.
DR   KEGG; bpt:Bpet2333; -.
DR   eggNOG; COG0625; Bacteria.
DR   Proteomes; UP000001225; Chromosome.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03057; GST_N_Beta; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13409; GST_N_2; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:CAP42676.1}.
FT   DOMAIN          1..83
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
SQ   SEQUENCE   212 AA;  23288 MW;  41C93953D3D332FC CRC64;
     MSTYELIGSR GCGSAIVEMA LELANVPYTV TDLPYLKPGP GRDRLLRLNV TGQVPTLVLP
     GGEVMTESAA MIMHLNDVAP AAGLAPPADS PERARFWHLL MRLIGAVYPT FTYADDPPKW
     TTAGEPAELL RTRVHGRRAE LWQELDRHVG APHVLGRRFS ALDLYVAVMI RWRPGPQWFK
     SCCPALYAAA QQAAGQPDVG QVLARHFDPP LE
//
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