GST26_SCHMA
ID GST26_SCHMA Reviewed; 218 AA.
AC P15964;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Glutathione S-transferase class-mu 26 kDa isozyme;
DE Short=GST 26;
DE EC=2.5.1.18;
DE AltName: Full=Sm26/1 antigen;
DE AltName: Full=SmGST;
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Puerto Rican;
RX PubMed=2385266; DOI=10.1016/0166-6851(90)90094-3;
RA Trottein F., Kieny M.P., Verwaerde C., Torpier G., Pierce R.J.,
RA Balloul J.-M., Schmitt D., Lecocq J.-P., Capron A.;
RT "Molecular cloning and tissue distribution of a 26-kilodalton Schistosoma
RT mansoni glutathione S-transferase.";
RL Mol. Biochem. Parasitol. 41:35-44(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-218.
RC STRAIN=Puerto Rican;
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 -!- TISSUE SPECIFICITY: Tegument and in subtegumentary parenchymal cells.
CC GST 26 may be actively excreted by adult worms.
CC -!- MISCELLANEOUS: There are at least three isoenzymes of GST in S.mansoni.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; M31106; AAA29888.1; -; mRNA.
DR EMBL; M26913; AAA29889.1; -; mRNA.
DR PIR; A45523; A45523.
DR AlphaFoldDB; P15964; -.
DR SMR; P15964; -.
DR STRING; 6183.Smp_163610.1; -.
DR PRIDE; P15964; -.
DR eggNOG; KOG1695; Eukaryota.
DR HOGENOM; CLU_039475_2_0_1; -.
DR BRENDA; 2.5.1.18; 5608.
DR Proteomes; UP000008854; Unassembled WGS sequence.
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; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Transferase.
FT CHAIN 1..218
FT /note="Glutathione S-transferase class-mu 26 kDa isozyme"
FT /id="PRO_0000185806"
FT DOMAIN 1..83
FT /note="GST N-terminal"
FT DOMAIN 85..203
FT /note="GST C-terminal"
FT BINDING 7..8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 41..45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 218 AA; 25401 MW; 061A6548A842D6E8 CRC64;
MAPKFGYWKV KGLVQPTRLL LEHLEETYEE RAYDRNEIDA WSNDKFKLGL EFPNLPYYID
GDFKLTQSMA IIRYIADKHN MLGACPKERA EISMLEGAVL DIRMGVLRIA YNKEYETLKV
DFLNKLPGRL KMFEDRLSNK TYLNGNCVTH PDFMLYDALD VVLYMDSQCL NEFPKLVSFK
KCIEDLPQIK NYLNSSRYIK WPLQGWDATF GGGDTPPK
