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Database: UniProt/TrEMBL
Entry: A9IN38_BORPD
LinkDB: A9IN38_BORPD
Original site: A9IN38_BORPD 
ID   A9IN38_BORPD            Unreviewed;       219 AA.
AC   A9IN38;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:CAP42783.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:CAP42783.1};
GN   OrderedLocusNames=Bpet2441 {ECO:0000313|EMBL:CAP42783.1};
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:CAP42783.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP42783.1, 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; CAP42783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IN38; -.
DR   STRING; 94624.Bpet2441; -.
DR   KEGG; bpt:Bpet2441; -.
DR   eggNOG; COG0625; Bacteria.
DR   OMA; YRAWFYP; -.
DR   Proteomes; UP000001225; Chromosome.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03188; GST_C_Beta; 1.
DR   CDD; cd03057; GST_N_Beta; 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; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051:SF10; GLUTATHIONE S-TRANSFERASE GSTA; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01150; Main.1:_Beta-like; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 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   Transferase {ECO:0000313|EMBL:CAP42783.1}.
FT   DOMAIN          3..84
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          90..218
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   219 AA;  24406 MW;  F67CB7B2A5EB5422 CRC64;
     MAKSVTKLFY FPGNASMAPH CLLEEIGQPF ELAFVDREQD AHKSADYLKL NPNGLIPVLV
     DGDMVLYESA AICLHLADRH PETKLAPACG TPQRAQLYKW LMWFTNTMQA TLLAYFYPER
     WVDEGNAAAA GQIKAHAEAK IAGLLDQMQA HLEKSGGPWF LGEQYTVLDP FAMMLCRWTR
     GHARPARDLP GLGAYLQRVL ARPAVQRALR TEGLAAPWV
//
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