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Database: UniProt
Entry: A9IHP1_BORPD
LinkDB: A9IHP1_BORPD
Original site: A9IHP1_BORPD 
ID   A9IHP1_BORPD            Unreviewed;       219 AA.
AC   A9IHP1;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Probable glutathione S-transferase {ECO:0000313|EMBL:CAP45260.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:CAP45260.1};
GN   OrderedLocusNames=Bpet4908 {ECO:0000313|EMBL:CAP45260.1};
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:CAP45260.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP45260.1, 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; CAP45260.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IHP1; -.
DR   STRING; 94624.Bpet4908; -.
DR   KEGG; bpt:Bpet4908; -.
DR   eggNOG; COG0625; Bacteria.
DR   Proteomes; UP000001225; Chromosome.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03194; GST_C_3; 1.
DR   CDD; cd03043; GST_N_1; 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; 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; PS50404; GST_NTER; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:CAP45260.1}.
FT   DOMAIN          2..82
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
SQ   SEQUENCE   219 AA;  24159 MW;  52CD3770D1A4D809 CRC64;
     MYTLIIGNKN YSSWSLRPWL ALRAAGIAFQ EQKLGLFTPE FAQRLGGITP AGLVPVLLDG
     DFAIWDSLAI CEYAAEQHPQ AGLWPADPRA RARARSLAAQ MHSGFGQLRQ VMPMNVEAHL
     PGIDISAAQG DVSRVQAIWH DTRAEFGQGG PFLFGRFSIA DAFYAPVVSR FTTYGVSAAG
     AVRDYMDAVL ALPAMREWTR EARTEGVFVP EDEPYRTQR
//
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