ID   GST28_SCHJA             Reviewed;         206 AA.
AC   P26624;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Glutathione S-transferase class-mu 28 kDa isozyme;
DE            Short=GST 28;
DE            EC=2.5.1.18;
DE   AltName: Full=Sj28 antigen;
DE   AltName: Full=Sj28GST;
DE   Flags: Fragment;
OS   Schistosoma japonicum (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6182;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sorsogon / Philippines;
RX   PubMed=1693415; DOI=10.1016/0166-6851(90)90076-x;
RA   Henkle K.J., Davern K.M., Wright M.D., Ramos A.J., Mitchell G.F.;
RT   "Comparison of the cloned genes of the 26- and 28-kilodalton glutathione S-
RT   transferases of Schistosoma japonicum and Schistosoma mansoni.";
RL   Mol. Biochem. Parasitol. 40:23-34(1990).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC   -!- FUNCTION: GST isoenzymes appear to play a central role in the parasite
CC       detoxification system. Other functions are also suspected including a
CC       role in increasing the solubility of haematin in the parasite gut.
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   -!- MISCELLANEOUS: There are at least two isoenzymes of GST in S.japonicum.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR   EMBL; M26914; AAA29890.1; -; mRNA.
DR   PIR; B44941; B44941.
DR   AlphaFoldDB; P26624; -.
DR   SMR; P26624; -.
DR   BRENDA; 2.5.1.18; 5607.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03192; GST_C_Sigma_like; 1.
DR   CDD; cd03039; GST_N_Sigma_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; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF224; HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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   2: Evidence at transcript level;
KW   Transferase.
FT   CHAIN           <1..206
FT                   /note="Glutathione S-transferase class-mu 28 kDa isozyme"
FT                   /id="PRO_0000185814"
FT   DOMAIN          <1..81
FT                   /note="GST N-terminal"
FT   DOMAIN          83..206
FT                   /note="GST C-terminal"
FT   BINDING         5..6
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         5
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         36..40
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         48
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT   BINDING         50..51
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   BINDING         65..66
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08515"
FT   NON_TER         1
SQ   SEQUENCE   206 AA;  23393 MW;  D1AD3707EDEABAA7 CRC64;
     VKLIYFNGRG RAEPIRMILV AAGVEFEDER IEFQDWPKIK PTIPGGRLPI VKITDKRGDV
     KTMSESLAIA RFIARKHNMM GDTDDEYYII EKMIGQVEDV ESEYHKTLIK PPEEKEKISK
     EILNGKVPIL LQAICETLKE STGNLTVGDK VTLADVVLIA SIDHITDLDK EFLTGKYPEI
     HKHRKHLLAT SPKLAKYLSE RHATAF
//