ID   GSTP2_BUFBU             Reviewed;         210 AA.
AC   P83325;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Glutathione S-transferase P 2;
DE            EC=2.5.1.18;
DE   AltName: Full=BBGSTP2-2;
DE   AltName: Full=GST class-pi;
OS   Bufo bufo (European toad) (Rana bufo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Bufo.
OX   NCBI_TaxID=8384;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=12127579; DOI=10.1016/s1357-2725(02)00066-3;
RA   Bucciarelli T., Sacchetta P., Amicarelli F., Petruzzelli R., Melino S.,
RA   Rotilio D., Celli N., Di Ilio C.;
RT   "Amino acid sequence of the major form of toad liver glutathione
RT   transferase.";
RL   Int. J. Biochem. Cell Biol. 34:1286-1290(2002).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000269|PubMed:12127579}.
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:12127579};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12127579}.
CC   -!- TISSUE SPECIFICITY: Liver, kidney, muscle, skin, lung and ovary.
CC       {ECO:0000269|PubMed:12127579}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}.
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DR   AlphaFoldDB; P83325; -.
DR   SMR; P83325; -.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03210; GST_C_Pi; 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; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR003082; GST_pi.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF141; GLUTATHIONE S-TRANSFERASE P; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01268; GSTRNSFRASEP.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Transferase.
FT   CHAIN           1..210
FT                   /note="Glutathione S-transferase P 2"
FT                   /id="PRO_0000185909"
FT   DOMAIN          1..82
FT                   /note="GST N-terminal"
FT   DOMAIN          83..204
FT                   /note="GST C-terminal"
FT   BINDING         7
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   BINDING         13
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   BINDING         38
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   BINDING         46
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   BINDING         53..54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   BINDING         66..67
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
SQ   SEQUENCE   210 AA;  24179 MW;  3D233F9AE53F3F8C CRC64;
     SGYTLTYFPL RGRAEAMRLL LGDQGVSWTD DEVQMQDWAA GIRDLKKNAV FGQIPRFQEG
     DFVLYQSQTI LRLLARYGLS GSNEREIAIN EMMNDGVEDL RLKYYKFIFW DNEANKEKFL
     EELATQLGYF ERILTNNAGK TFVLVGDKIS YADYNLLDTL FCVLDLSPTC LSGFPLLSDY
     VERLGKRPKL QQYLKSEGRK RRPINGNGKQ
//