ID   Q72U57_LEPIC            Unreviewed;       164 AA.
AC   Q72U57;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:AAS69421.1};
GN   Name=gst {ECO:0000313|EMBL:AAS69421.1};
GN   OrderedLocusNames=LIC_10807 {ECO:0000313|EMBL:AAS69421.1};
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=267671 {ECO:0000313|EMBL:AAS69421.1, ECO:0000313|Proteomes:UP000007037};
RN   [1] {ECO:0000313|EMBL:AAS69421.1, ECO:0000313|Proteomes:UP000007037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130 {ECO:0000313|EMBL:AAS69421.1,
RC   ECO:0000313|Proteomes:UP000007037};
RX   PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004;
RA   Nascimento A.L., Ko A.I., Martins E.A., Monteiro-Vitorello C.B., Ho P.L.,
RA   Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F., Leite L.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H., Harakava R., Jeronimo S.M., Junqueira-De-Azevedo I.L.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G., Lemos M.V., Marino C.L., Nunes L.R.,
RA   De Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J.,
RA   Sommer P., Tsai S.M., Simpson A.J., Ferro J.A., Camargo L.E.,
RA   Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
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DR   EMBL; AE016823; AAS69421.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q72U57; -.
DR   KEGG; lic:LIC_10807; -.
DR   HOGENOM; CLU_011226_14_4_12; -.
DR   Proteomes; UP000007037; Chromosome I.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 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:AAS69421.1}.
FT   DOMAIN          1..83
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          86..164
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   164 AA;  18604 MW;  4AB63CD57E87C8A1 CRC64;
     MIELYSASTP NGRKISIMLE ELGIPYTVHP INLDKLEQKQ EWFLKINPNG RIPAIIDKDN
     EDFTVFESGA ILIYLAEKTG KLLPKDPKEK STVIQWLMFQ MGGVGPMQGQ AGVFLKYAPE
     KIPFAINRYQ NETKRLYSVL DRRLSDSKFL GGKDLSIADI ATWP
//