ID B0VLH9_ACIBS Unreviewed; 203 AA. AC B0VLH9; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 84. DE SubName: Full=Glutathionine S-transferase {ECO:0000313|EMBL:CAP00828.1}; DE EC=2.5.1.18 {ECO:0000313|EMBL:CAP00828.1}; GN OrderedLocusNames=ABSDF1484 {ECO:0000313|EMBL:CAP00828.1}; OS Acinetobacter baumannii (strain SDF). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP00828.1, ECO:0000313|Proteomes:UP000001741}; RN [1] {ECO:0000313|EMBL:CAP00828.1, ECO:0000313|Proteomes:UP000001741} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SDF {ECO:0000313|EMBL:CAP00828.1, RC ECO:0000313|Proteomes:UP000001741}; RX PubMed=18350144; DOI=10.1371/journal.pone.0001805; RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., RA Weissenbach J., Cruveiller S.; RT "Comparative analysis of Acinetobacters: three genomes for three RT lifestyles."; RL PLoS ONE 3:E1805-E1805(2008). CC -!- SIMILARITY: Belongs to the GST superfamily. CC {ECO:0000256|RuleBase:RU003494}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU468230; CAP00828.1; -; Genomic_DNA. DR AlphaFoldDB; B0VLH9; -. DR KEGG; abm:ABSDF1484; -. DR HOGENOM; CLU_011226_6_1_6; -. DR BioCyc; ABAU509170:GCL9-1207-MONOMER; -. DR Proteomes; UP000001741; Chromosome. 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; 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: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; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG01150; Main.1:_Beta-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 Transferase {ECO:0000313|EMBL:CAP00828.1}. 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; 22977 MW; C27AF6BEFA15F152 CRC64; MKLYYSPGAC SLAAHIILNE INVDFDLERV NLKTHKTEKG ADYYEINPKG YVPALEINPG LILTENVAIL PFLAQHDPKQ DLIPPSGLGR AKVLEWLGYL NSELHDAYAV FFGAPLTNDE KTKAYAEIDR LLKYIDNYLA ESDYDYLVND NFGPADAYLF VLTNWSNSIE HDLTPYKHII ALRNKVAERQ SVQIAMRDEG LIS //