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Database: UniProt
Entry: D0SVY7_ACILW
LinkDB: D0SVY7_ACILW
Original site: D0SVY7_ACILW 
ID   D0SVY7_ACILW            Unreviewed;       203 AA.
AC   D0SVY7;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:EEY90044.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:EEY90044.1};
GN   Name=gst {ECO:0000313|EMBL:EEY90044.1};
GN   ORFNames=HMPREF0017_01461 {ECO:0000313|EMBL:EEY90044.1};
OS   Acinetobacter lwoffii SH145.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=575588 {ECO:0000313|EMBL:EEY90044.1, ECO:0000313|Proteomes:UP000018425};
RN   [1] {ECO:0000313|Proteomes:UP000018425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH145 {ECO:0000313|Proteomes:UP000018425};
RX   PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA   Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA   Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA   Seifert H., Dijkshoorn L.;
RT   "The success of Acinetobacter species; genetic, metabolic and virulence
RT   attributes.";
RL   PLoS ONE 7:E46984-E46984(2012).
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; GG705059; EEY90044.1; -; Genomic_DNA.
DR   RefSeq; WP_004280108.1; NZ_GG705059.1.
DR   AlphaFoldDB; D0SVY7; -.
DR   GeneID; 69582525; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_6_1_6; -.
DR   Proteomes; UP000018425; Unassembled WGS sequence.
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; PF00043; GST_C; 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   3: Inferred from homology;
KW   Transferase {ECO:0000313|EMBL:EEY90044.1}.
FT   DOMAIN          1..81
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          86..203
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   203 AA;  22956 MW;  03889559A11E1EBC CRC64;
     MKLYYSPGAC SLAAHIILNE INVDFDLERV DLKTHKTEKG TDYYEVNPKG YVPALEINPG
     LILTENVAIL PFLAQHDPKQ DLIPPSGMGR AKVLEWLGYL NSELHDAYAV FFGGKLSEDE
     KKKAYAEIDR LLSYIDKAIG ESDNDYLVDD NFGPADAYLF VLTNWSNQIE HDLSPYKNII
     HIRNKVAERQ SVQIAMRDEG LIP
//
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