ID   GSTP1_BUFBU             Reviewed;         210 AA.
AC   P81942;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Glutathione S-transferase P 1;
DE            EC=2.5.1.18;
DE   AltName: Full=BBGSTP1-1;
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.
RC   TISSUE=Embryo;
RX   PubMed=9065793; DOI=10.1042/bj3220679;
RA   Sacchetta P., Petruzzelli R., Melino S., Bucciarelli T., Pennelli A.,
RA   Amicarelli F., Miranda M., Di Ilio C.;
RT   "Amphibian embryo glutathione transferase: amino acid sequence and
RT   structural properties.";
RL   Biochem. J. 322:679-680(1997).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
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   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion
CC       {ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino
CC       acids function as un uncleaved transit peptide, and arginine residues
CC       within it are crucial for mitochondrial localization. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}.
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DR   AlphaFoldDB; P81942; -.
DR   SMR; P81942; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03210; GST_C_Pi; 1.
DR   CDD; cd03076; GST_N_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   Cytoplasm; Direct protein sequencing; Mitochondrion; Nucleus; Transferase.
FT   CHAIN           1..210
FT                   /note="Glutathione S-transferase P 1"
FT                   /id="PRO_0000185908"
FT   DOMAIN          1..80
FT                   /note="GST N-terminal"
FT   DOMAIN          82..203
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         44
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   BINDING         51..52
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   BINDING         64..65
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
SQ   SEQUENCE   210 AA;  23820 MW;  AC835C0390F3A71D CRC64;
     PEYTIIYFNA RGRCEAMRML MADQGAQWKE EVVTSDDWQK GDLKKAAVYG QLPGFKDGDF
     TLYQSNAMLR LLARNHDLYG KNPREASLID MVNDGVEDLR LKYLKMIYQN YENGKDDYVK
     ALPTNLGHFE RLLASNNEGK GFVVGAHISF ADYNLVDLLH NHLVLAPDCL SGFPLLCAYV
     KRISSRPKLE AYLSSDAHKK RPINGNGKQQ
//