ID B2FLE2_STRMK Unreviewed; 218 AA. AC B2FLE2; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 78. DE SubName: Full=Glutathione S-transferase protein {ECO:0000313|EMBL:CAQ46649.1}; GN OrderedLocusNames=Smlt3208 {ECO:0000313|EMBL:CAQ46649.1}; OS Stenotrophomonas maltophilia (strain K279a). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group. OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ46649.1, ECO:0000313|Proteomes:UP000008840}; RN [1] {ECO:0000313|EMBL:CAQ46649.1, ECO:0000313|Proteomes:UP000008840} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K279a {ECO:0000313|EMBL:CAQ46649.1, RC ECO:0000313|Proteomes:UP000008840}; RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74; RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D., RA Parkhill J., Thomson N.R., Avison M.B.; RT "The complete genome, comparative and functional analysis of RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug RT resistance determinants."; RL Genome Biol. 9:R74.1-R74.13(2008). 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; AM743169; CAQ46649.1; -; Genomic_DNA. DR RefSeq; WP_005410282.1; NC_010943.1. DR AlphaFoldDB; B2FLE2; -. DR EnsemblBacteria; CAQ46649; CAQ46649; Smlt3208. DR GeneID; 61466707; -. DR KEGG; sml:Smlt3208; -. DR eggNOG; COG0625; Bacteria. DR HOGENOM; CLU_011226_6_0_6; -. DR Proteomes; UP000008840; Chromosome. 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; PF13409; GST_N_2; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG01150; Main.1:_Beta-like; 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 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000008840}. FT DOMAIN 6..88 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 90..215 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" SQ SEQUENCE 218 AA; 24565 MW; 8DACD532D2665D68 CRC64; MVEERVPLTV HGMSVSGNCH KVRLLLEQLG SRYRWVEVDS AHGQTHTPEF LALNPNAKVP LIVRDDGRVL TESNAILFWL AEGTPYLPSD GWERAQALSW MFFEQYTHEP CVAVARFIRG WTAPDSPRRA ELPRLHERAA TALAVMEQHL REAQWFTGSG YGIADIALFA YTDVAGEGGI SLEPFPEVRA WLQRVRAQPR FLPMPAVTAE VRSRFEAA //