ID B1LEX5_ECOSM Unreviewed; 288 AA.
AC B1LEX5;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:ACB19479.1};
DE EC=2.5.1.18 {ECO:0000313|EMBL:ACB19479.1};
GN OrderedLocusNames=EcSMS35_3275 {ECO:0000313|EMBL:ACB19479.1};
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB19479.1, ECO:0000313|Proteomes:UP000007011};
RN [1] {ECO:0000313|EMBL:ACB19479.1, ECO:0000313|Proteomes:UP000007011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
RX PubMed=18708504; DOI=10.1128/JB.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
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DR EMBL; CP000970; ACB19479.1; -; Genomic_DNA.
DR RefSeq; WP_000131798.1; NC_010498.1.
DR AlphaFoldDB; B1LEX5; -.
DR GeneID; 83579463; -.
DR KEGG; ecm:EcSMS35_3275; -.
DR HOGENOM; CLU_011226_14_4_6; -.
DR Proteomes; UP000007011; Chromosome.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR CDD; cd10292; GST_C_YghU_like; 1.
DR CDD; cd03048; GST_N_Ure2p_like; 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; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR44051:SF8; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR Pfam; PF13410; GST_C_2; 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 4: Predicted;
KW Transferase {ECO:0000313|EMBL:ACB19479.1}.
FT DOMAIN 46..133
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 139..265
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 260..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 288 AA; 32374 MW; 385077B20A3C1D99 CRC64;
MTDNTYQPAK VWTWDKSAGG AFANINRPVS GPTHEKTLPV GKHPLQLYSL GTPNGQKVTI
MLEELLALGV TGAEYDAWLI RIGDGDQFSS GFVEVNPNSK IPALRDHTHN PPIRVFESGS
ILLYLAEKFG YFLPQDLAKR TETLNWLFWL QGAAPFLGGG FGHFYHYAPV KIEYAINRFT
MEAKRLLDVL DKQLAQHKFV AGDEYTIADM AIWPWFGNVV LGGVYDAAEF LDAGSYKHVQ
RWAKEVGERP AVKRGRIVNR TNGPLNEQLH ERHDASDFET NTEDKRQG
//
