GSTB_SHIFL
ID GSTB_SHIFL Reviewed; 208 AA.
AC P0ACA9; P75805; Q9R7R4;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Glutathione S-transferase GstB;
DE EC=2.5.1.18;
GN Name=gstB; OrderedLocusNames=SF0788, S0831;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN42421.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP16296.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AE005674; AAN42421.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP16296.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_706714.1; NC_004337.2.
DR RefSeq; WP_001295292.1; NZ_WPGW01000151.1.
DR AlphaFoldDB; P0ACA9; -.
DR SMR; P0ACA9; -.
DR STRING; 198214.SF0788; -.
DR PRIDE; P0ACA9; -.
DR EnsemblBacteria; AAN42421; AAN42421; SF0788.
DR EnsemblBacteria; AAP16296; AAP16296; S0831.
DR GeneID; 1023726; -.
DR GeneID; 66670888; -.
DR KEGG; sfl:SF0788; -.
DR KEGG; sfx:S0831; -.
DR PATRIC; fig|198214.7.peg.915; -.
DR HOGENOM; CLU_011226_6_2_6; -.
DR OrthoDB; 1752966at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
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 Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Reference proteome; Transferase.
FT CHAIN 1..208
FT /note="Glutathione S-transferase GstB"
FT /id="PRO_0000186020"
FT DOMAIN 1..83
FT /note="GST N-terminal"
FT DOMAIN 88..208
FT /note="GST C-terminal"
FT BINDING 12
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
SQ SEQUENCE 208 AA; 23713 MW; 8AD199E313B05094 CRC64;
MITLWGRNNS TNVKKVLLTL EELELPYEQI LAGREFGINH DADFLAMNPN GLVPLLRDDE
SDLILWESNA IVRYLAAQYG QKRLWIDSPA RRAEAEKWMD WANQTLSNAH RGILMGLVRT
PPEERDQAAI DASCKECDAL FALLDAELAK VKWFSGDEFG VGDIAIAPFI YNLFNVGLTW
TPRPNLQRWY QQLTERPAVR KVVMIPVS
