GSTB_ECOLI
ID GSTB_ECOLI Reviewed; 208 AA.
AC P0ACA7; P75805; Q9R7R4;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Glutathione S-transferase GstB;
DE EC=2.5.1.18;
GN Name=gstB; Synonyms=yliJ; OrderedLocusNames=b0838, JW0822;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, AND GENE NAME.
RX PubMed=20921376; DOI=10.1073/pnas.1007559107;
RA Desai K.K., Miller B.G.;
RT "Recruitment of genes and enzymes conferring resistance to the nonnatural
RT toxin bromoacetate.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17968-17973(2010).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Catalyzes the
CC glutathione-dependent dehalogenation of bromoacetate.
CC {ECO:0000269|PubMed:20921376}.
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 Evidence={ECO:0000269|PubMed:20921376};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 mM for bromoacetate {ECO:0000269|PubMed:20921376};
CC -!- INTERACTION:
CC P0ACA7; P0ACA7: gstB; NbExp=2; IntAct=EBI-1120568, EBI-1120568;
CC P0ACA7; P06987: hisB; NbExp=4; IntAct=EBI-1120568, EBI-1126930;
CC -!- DISRUPTION PHENOTYPE: Mutants are hypersensitive to bromoacetate.
CC {ECO:0000269|PubMed:20921376}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC73925.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35541.1; -; Genomic_DNA.
DR RefSeq; NP_415359.4; NC_000913.3.
DR RefSeq; WP_001295292.1; NZ_STEB01000019.1.
DR AlphaFoldDB; P0ACA7; -.
DR SMR; P0ACA7; -.
DR BioGRID; 4262824; 14.
DR BioGRID; 849843; 2.
DR DIP; DIP-48220N; -.
DR IntAct; P0ACA7; 2.
DR STRING; 511145.b0838; -.
DR jPOST; P0ACA7; -.
DR PaxDb; P0ACA7; -.
DR PRIDE; P0ACA7; -.
DR EnsemblBacteria; AAC73925; AAC73925; b0838.
DR EnsemblBacteria; BAA35541; BAA35541; BAA35541.
DR GeneID; 66670888; -.
DR GeneID; 945469; -.
DR KEGG; ecj:JW0822; -.
DR KEGG; eco:b0838; -.
DR PATRIC; fig|1411691.4.peg.1440; -.
DR EchoBASE; EB3254; -.
DR eggNOG; COG0625; Bacteria.
DR HOGENOM; CLU_011226_6_2_6; -.
DR InParanoid; P0ACA7; -.
DR OMA; LWQKAFE; -.
DR PhylomeDB; P0ACA7; -.
DR BioCyc; EcoCyc:G6438-MON; -.
DR BioCyc; MetaCyc:G6438-MON; -.
DR SABIO-RK; P0ACA7; -.
DR PRO; PR:P0ACA7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0030611; F:arsenate reductase activity; IDA:EcoCyc.
DR GO; GO:0043295; F:glutathione binding; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..208
FT /note="Glutathione S-transferase GstB"
FT /id="PRO_0000186018"
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
