ID GSTM1_CAVPO Reviewed; 217 AA.
AC P16413;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 22-FEB-2023, entry version 114.
DE RecName: Full=Glutathione S-transferase B {ECO:0000305};
DE Short=GST B;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P09488};
DE AltName: Full=GST class-mu;
GN Name=GSTM1;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2332413; DOI=10.1093/oxfordjournals.jbchem.a122992;
RA Kamei K., Oshino R., Hara S.;
RT "Amino acid sequence of glutathione S-transferase b from guinea pig
RT liver.";
RL J. Biochem. 107:111-117(1990).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Involved in the
CC formation of glutathione conjugates of both prostaglandin A2 (PGA2) and
CC prostaglandin J2 (PGJ2). Participates in the formation of novel
CC hepoxilin regioisomers. {ECO:0000250|UniProtKB:P09488}.
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:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50796, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133370, ChEBI:CHEBI:133768;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50797;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133771;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(S)-
CC glutathione; Xref=Rhea:RHEA:50808, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133772;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50809;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(S)-
CC glutathione; Xref=Rhea:RHEA:50800, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133370, ChEBI:CHEBI:133769;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50801;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate +
CC glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)-
CC eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:132200, ChEBI:CHEBI:132201;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261;
CC Evidence={ECO:0000250|UniProtKB:P09488};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR PIR; JX0095; JX0095.
DR AlphaFoldDB; P16413; -.
DR SMR; P16413; -.
DR STRING; 10141.ENSCPOP00000007027; -.
DR eggNOG; KOG1695; Eukaryota.
DR InParanoid; P16413; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR GO; GO:1901687; P:glutathione derivative biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR CDD; cd03209; GST_C_Mu; 1.
DR CDD; cd03075; GST_N_Mu; 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; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF126; GLUTATHIONE S-TRANSFERASE MU 1; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
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; Lipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..217
FT /note="Glutathione S-transferase B"
FT /id="PRO_0000185834"
FT DOMAIN 1..87
FT /note="GST N-terminal"
FT DOMAIN 89..207
FT /note="GST C-terminal"
FT BINDING 6..7
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 45..49
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 58..59
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 71..72
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 217 AA; 25719 MW; D29F7951D4E9365E CRC64;
PMTLGYWNIR GLTHPIRLIL EYTNSGYEEK RYNMGDAPDY DRSQWLNEKF KLGLDFPNLP
YLIDGTHKLT QSNAILRYIA RKHNLCGVTE EETIRMDILE NQVMDIRMQL IMLCYSPDFE
QKKAEFLEGI PDKMKLFSQF LGKLPWFAGN KLTYVDFLAY DVLDQYRMLE PKCLEAFPNL
KDFISRFEGL EKISSYMKSS RFLPKPLFSK FAFWNNK
//
