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Database: UniProt
Entry: Q8D0L3
LinkDB: Q8D0L3
Original site: Q8D0L3 
ID   Q8D0L3_YERPE            Unreviewed;       202 AA.
AC   Q8D0L3; Q74TK2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   07-APR-2021, entry version 133.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:AAS62361.1};
DE   SubName: Full=Glutathionine S-transferase {ECO:0000313|EMBL:AAM85534.1};
GN   Name=gst {ECO:0000313|EMBL:AAM85534.1};
GN   Synonyms=gst2 {ECO:0000313|EMBL:AAS62361.1};
GN   OrderedLocusNames=y1968 {ECO:0000313|EMBL:AAM85534.1}, YP_2153
GN   {ECO:0000313|EMBL:AAS62361.1};
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632 {ECO:0000313|EMBL:AAM85534.1, ECO:0000313|Proteomes:UP000002490};
RN   [1] {ECO:0000313|EMBL:AAM85534.1, ECO:0000313|Proteomes:UP000002490}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM {ECO:0000313|EMBL:AAM85534.1}, and KIM10+ / Biovar
RC   Mediaevalis {ECO:0000313|Proteomes:UP000002490};
RX   PubMed=12142430; DOI=10.1128/JB.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G.III., Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plana G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [2] {ECO:0000313|EMBL:AAS62361.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=91001 {ECO:0000313|EMBL:AAS62361.1};
RA   Waterston R.H.;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis {ECO:0000313|Proteomes:UP000001019};
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
RN   [4] {ECO:0007829|PDB:4GCI}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RG   Enzyme Function Initiative (EFI);
RA   Vetting M.W., Toro R., Bhosle R., Al Obaidi N.F., Morisco L.L.,
RA   Wasserman S.R., Sojitra S., Washington E., Scott Glenn A., Chowdhury S.,
RA   Evans B., Hammonds J., Hillerich B., Love J., Seidel R.D., Imker H.J.,
RA   Armstrong R.N., Gerlt J.A., Almo S.C.;
RT   "Crystal structure of glutahtione s-transferase homolog from yersinia
RT   pestis, target EFI-501894, with bound glutathione, monoclinic form.";
RL   Submitted (JUL-2012) to the PDB data bank.
RN   [5] {ECO:0007829|PDB:4G9H}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RG   Enzyme Function Initiative (EFI);
RA   Vetting M.W., Toro R., Bhosle R., Al Obaidi N.F., Morisco L.L.,
RA   Wasserman S.R., Sojitra S., Washington E., Scott Glenn A., Chowdhury S.,
RA   Evans B., Hammonds J., Hillerich B., Love J., Seidel R.D., Imker H.J.,
RA   Armstrong R.N., Gerlt J.A., Almo S.C.;
RT   "Crystal structure of glutahtione s-transferase homolog from yersinia
RT   pestis, target efi-501894, with bound glutathione.";
RL   Submitted (JUL-2012) to the PDB data bank.
RN   [6] {ECO:0000313|EMBL:AAS62361.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=91001 {ECO:0000313|EMBL:AAS62361.1};
RA   Yiqing M.;
RT   "Reannotation of Yersinia pestis strain 91001 based on omics data.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; AE009952; AAM85534.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS62361.1; -; Genomic_DNA.
DR   PDB; 4G9H; X-ray; 2.10 A; A/B=1-202.
DR   PDB; 4GCI; X-ray; 1.50 A; A/B=1-202.
DR   PDBsum; 4G9H; -.
DR   PDBsum; 4GCI; -.
DR   SMR; Q8D0L3; -.
DR   IntAct; Q8D0L3; 1.
DR   DNASU; 1146915; -.
DR   EnsemblBacteria; AAM85534; AAM85534; y1968.
DR   EnsemblBacteria; AAS62361; AAS62361; YP_2153.
DR   KEGG; ypk:y1968; -.
DR   KEGG; ypm:YP_2153; -.
DR   HOGENOM; CLU_011226_6_1_6; -.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.30.10; -; 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   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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   3D-structure {ECO:0007829|PDB:4G9H, ECO:0007829|PDB:4GCI};
KW   Transferase {ECO:0000313|EMBL:AAM85534.1}.
FT   DOMAIN          1..82
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          88..202
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          66..67
FT                   /note="Glutathione 2 binding"
FT                   /evidence="ECO:0007829|PDB:4G9H"
FT   REGION          104..105
FT                   /note="Glutathione 2 binding"
FT                   /evidence="ECO:0007829|PDB:4G9H"
FT   REGION          104..105
FT                   /note="Glutathione 3 binding"
FT                   /evidence="ECO:0007829|PDB:4GCI"
FT   BINDING         11
FT                   /note="Glutathione 1; via amide nitrogen"
FT                   /evidence="ECO:0007829|PDB:4GCI"
FT   BINDING         36
FT                   /note="Glutathione 1"
FT                   /evidence="ECO:0007829|PDB:4GCI"
FT   BINDING         36
FT                   /note="Glutathione 2"
FT                   /evidence="ECO:0007829|PDB:4G9H"
FT   BINDING         53
FT                   /note="Glutathione 1; via amide nitrogen and carbonyl
FT                   oxygen"
FT                   /evidence="ECO:0007829|PDB:4GCI"
FT   BINDING         53
FT                   /note="Glutathione 2; via amide nitrogen and carbonyl
FT                   oxygen"
FT                   /evidence="ECO:0007829|PDB:4G9H"
FT   BINDING         66
FT                   /note="Glutathione 1"
FT                   /evidence="ECO:0007829|PDB:4GCI"
FT   BINDING         100
FT                   /note="Glutathione 2"
FT                   /evidence="ECO:0007829|PDB:4G9H"
FT   BINDING         100
FT                   /note="Glutathione 3"
FT                   /evidence="ECO:0007829|PDB:4GCI"
SQ   SEQUENCE   202 AA;  22665 MW;  B617432BCD858B65 CRC64;
     MMKLFYKPGA CSLSPHIVLR EAGLDFSIER VDLVTKKTET GADYLSINPK GQVPALVLDD
     GSLLTEGVAI VQYLADKVPD RHLIAPSGTL SRYHAIEWLN FIATELHKGF SPLFNPNTPD
     EYKTIVRERL DKQFSYVDSV LAEHDYLLGK KFSVADAYLF TVSRWANALN LQIKERSHLD
     QYMARVAERP AVKAALAAED IK
//
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