ID   Q6FG07_ACIAD            Unreviewed;       204 AA.
AC   Q6FG07;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   04-NOV-2026, entry version 126.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:CAG67000.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:CAG67000.1};
GN   OrderedLocusNames=ACIAD0017 {ECO:0000313|EMBL:CAG67000.1};
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Moraxellales; Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG67000.1, ECO:0000313|Proteomes:UP000000430};
RN   [1] {ECO:0000313|EMBL:CAG67000.1, ECO:0000313|Proteomes:UP000000430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; CR543861; CAG67000.1; -; Genomic_DNA.
DR   RefSeq; WP_004930985.1; NC_005966.1.
DR   AlphaFoldDB; Q6FG07; -.
DR   STRING; 202950.GCA_001485005_01765; -.
DR   GeneID; 45232551; -.
DR   KEGG; aci:ACIAD0017; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_6_0_6; -.
DR   OMA; AAKMDEW; -.
DR   OrthoDB; 9797500at2; -.
DR   BioCyc; ASP62977:ACIAD_RS00095-MONOMER; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03056; GST_N_4; 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; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR44051:SF2; HYPOTHETICAL GLUTATHIONE S-TRANSFERASE LIKE PROTEIN; 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   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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000430};
KW   Transferase {ECO:0000313|EMBL:CAG67000.1}.
FT   DOMAIN          1..81
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          83..204
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   204 AA;  23353 MW;  13AEB1E4A92DE70B CRC64;
     MKVYGDIQSG NCYKVKLLLN FLELAHEWIH IDVLKAETHT PEFLKMNPNA KIPVVQLEDG
     QLLAESNAIL GYLAEGTHFI PSDRYKKAKM YEWMFFEQYS HEPCIAVARF IQKYQGMPEA
     RLEEYQKLQP KGHKVLAILE QALDGHHYLL GEEVSLADIS LYAYTHVADE GGFDLNLYPN
     IQRWCQRIAN SAGYVGMNTQ TTAV
//