ID Q6FG07_ACIAD Unreviewed; 204 AA.
AC Q6FG07;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=Putative 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; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC 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 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 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
//