GSTP2_BUFBU
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 03-AUG-2022, entry version 69.
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).
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 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; IPR003082; GST_pi.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01268; GSTRNSFRASEP.
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 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