ID   GST27_SCHMA             Reviewed;         195 AA.
AC   P35661; G4VKM5;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 2.
DT   04-NOV-2026, entry version 117.
DE   RecName: Full=Glutathione S-transferase class-mu 26 kDa isozyme;
DE            Short=GST 26;
DE            EC=2.5.1.18;
DE   AltName: Full=Sm26/2 antigen;
GN   ORFNames=Smp_102070;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Neodermata; Trematoda; Digenea; Strigeidida;
OC   Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1775156; DOI=10.1016/0166-6851(91)90140-2;
RA   Wright M.D., Harrison R.A., Melder A.M., Newport G.R., Mitchell G.F.;
RT   "Another 26-kilodalton glutathione S-transferase of Schistosoma mansoni.";
RL   Mol. Biochem. Parasitol. 49:177-179(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Puerto Rican;
RX   PubMed=19606141; DOI=10.1038/nature08160;
RA   Berriman M., Haas B.J., LoVerde P.T., Wilson R.A., Dillon G.P.,
RA   Cerqueira G.C., Mashiyama S.T., Al-Lazikani B., Andrade L.F., Ashton P.D.,
RA   Aslett M.A., Bartholomeu D.C., Blandin G., Caffrey C.R., Coghlan A.,
RA   Coulson R., Day T.A., Delcher A., DeMarco R., Djikeng A., Eyre T.,
RA   Gamble J.A., Ghedin E., Gu Y., Hertz-Fowler C., Hirai H., Hirai Y.,
RA   Houston R., Ivens A., Johnston D.A., Lacerda D., Macedo C.D., McVeigh P.,
RA   Ning Z., Oliveira G., Overington J.P., Parkhill J., Pertea M., Pierce R.J.,
RA   Protasio A.V., Quail M.A., Rajandream M.A., Rogers J., Sajid M.,
RA   Salzberg S.L., Stanke M., Tivey A.R., White O., Williams D.L., Wortman J.,
RA   Wu W., Zamanian M., Zerlotini A., Fraser-Liggett C.M., Barrell B.G.,
RA   El-Sayed N.M.;
RT   "The genome of the blood fluke Schistosoma mansoni.";
RL   Nature 460:352-358(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Puerto Rican;
RX   PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA   Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA   De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA   Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA   Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA   Zerlotini A., Dunne D.W., Berriman M.;
RT   "A systematically improved high quality genome and transcriptome of the
RT   human blood fluke Schistosoma mansoni.";
RL   PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
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=RX + glutathione = an S-substituted glutathione + a halide
CC         anion + 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   -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR   EMBL; M73624; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; HE601628; CCD80234.1; -; Genomic_DNA.
DR   PIR; A45556; A45556.
DR   RefSeq; XP_018652834.1; XM_018797832.1.
DR   AlphaFoldDB; P35661; -.
DR   SMR; P35661; -.
DR   STRING; 6183.P35661; -.
DR   GeneID; 8348519; -.
DR   KEGG; smm:Smp_102070; -.
DR   CTD; 8348519; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   HOGENOM; CLU_039475_2_0_1; -.
DR   InParanoid; P35661; -.
DR   OMA; AAMWGNK; -.
DR   OrthoDB; 4951845at2759; -.
DR   PhylomeDB; P35661; -.
DR   Proteomes; UP000008854; Chromosome 5.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:TreeGrafter.
DR   GO; GO:0042178; P:xenobiotic catabolic process; IEA:UniProtKB-ARBA.
DR   CDD; cd03075; GST_N_Mu; 1.
DR   Gene3D; 1.20.1050.130; -; 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; IPR050213; GST_superfamily.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF222; GLUTATHIONE TRANSFERASE; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 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   Reference proteome; Transferase.
FT   CHAIN           1..195
FT                   /note="Glutathione S-transferase class-mu 26 kDa isozyme"
FT                   /id="PRO_0000185811"
FT   DOMAIN          1..83
FT                   /note="GST N-terminal"
FT   DOMAIN          85..195
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   195 AA;  22546 MW;  7FF9CA7AB3E445B9 CRC64;
     MAPKLGYWKI KGLVQPTRLL LEYLGEAYEE RLYDRNDGDV WRNEKFKLGL DFPNLPYYID
     GDVKLTQSMA ILRYIADKHN MLGGCPKERA EISMLEGAIL DIRYGVSRIA YNKEFETLKV
     DFLNQLPGML KMFEDRLSHN TYLNGDKVTH PDFMLYDALD VNLPPIKNYL NSNRYIKWPL
     QGWSATFGGG DAPPK
//