ID   C5A7Z5_BURGB            Unreviewed;       211 AA.
AC   C5A7Z5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:ACR29239.1};
GN   OrderedLocusNames=bglu_1g21330 {ECO:0000313|EMBL:ACR29239.1};
OS   Burkholderia glumae (strain BGR1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR29239.1, ECO:0000313|Proteomes:UP000002187};
RN   [1] {ECO:0000313|EMBL:ACR29239.1, ECO:0000313|Proteomes:UP000002187}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGR1 {ECO:0000313|EMBL:ACR29239.1,
RC   ECO:0000313|Proteomes:UP000002187};
RX   PubMed=19329631; DOI=10.1128/JB.00349-09;
RA   Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT   "Complete genome sequence of Burkholderia glumae BGR1.";
RL   J. Bacteriol. 191:3758-3759(2009).
RN   [2] {ECO:0007829|PDB:4ISD}
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, AND
RP   DISULFIDE BONDS.
RG   Enzyme Function Initiative (EFI);
RA   Vetting M.W., Toro R., Bhosle R., Al Obaidi N.F., Morisco L.L.,
RA   Wasserman S.R., Sojitra S., Washington E., Scott Glenn A., Chowdhury S.,
RA   Evans B., Hammonds J., Hillerich B., Love J., Seidel R.D., Imker H.J.,
RA   Armstrong R.N., Gerlt J.A., Almo S.C.;
RT   "Crystal structure of GLUTATHIONE TRANSFERASE homolog from BURKHOLDERIA GL
RT   BGR1, TARGET EFI-501803, with bound glutathione.";
RL   Submitted (JAN-2013) to the PDB data bank.
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DR   EMBL; CP001503; ACR29239.1; -; Genomic_DNA.
DR   RefSeq; WP_015876122.1; NC_012724.2.
DR   PDB; 4ISD; X-ray; 2.65 A; A/B/C/D/E=1-211.
DR   PDBsum; 4ISD; -.
DR   AlphaFoldDB; C5A7Z5; -.
DR   SMR; C5A7Z5; -.
DR   STRING; 626418.bglu_1g21330; -.
DR   GeneID; 58134467; -.
DR   KEGG; bgl:bglu_1g21330; -.
DR   PATRIC; fig|626418.3.peg.4944; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_17_0_4; -.
DR   Proteomes; UP000002187; Chromosome 1.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd03195; GST_C_4; 1.
DR   CDD; cd00570; GST_N_family; 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; IPR034338; GST_4_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1.
DR   PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 1.
DR   Pfam; PF14834; GST_C_4; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4ISD};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002187};
KW   Transferase {ECO:0000313|EMBL:ACR29239.1}.
FT   DOMAIN          6..87
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   BINDING         44
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0007829|PDB:4ISD"
FT   BINDING         59
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0007829|PDB:4ISD"
FT   BINDING         72
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0007829|PDB:4ISD"
FT   BINDING         110
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0007829|PDB:4ISD"
FT   DISULFID        142..181
FT                   /evidence="ECO:0007829|PDB:4ISD"
SQ   SEQUENCE   211 AA;  24109 MW;  A3B87EEAD437943A CRC64;
     MSQKPITLYV GADYVSAFAM SAFVVLKEKG LDFEIRTVDL KSKQQHGSAY REVSLTRRVP
     TLQHDRFTLS ESSAIAEYLD EVYPAPHYAA VLPADRETRA LARQLQAWIR SDFMPLKSER
     QADRIYFPEP VKPLGEAAQL ACEKLLSAAD RLIDDERYGV FGDWCIADTD FALMLNRLVA
     CGDPVPPKVL RYVERQWARP SVQQWVKQKR D
//