ID   GST26_SCHJA             Reviewed;         218 AA.
AC   P08515;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Glutathione S-transferase class-mu 26 kDa isozyme;
DE            Short=GST 26;
DE            EC=2.5.1.18;
DE   AltName: Full=Sj26 antigen;
DE   AltName: Full=SjGST;
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].
RX   PubMed=3095841; DOI=10.1073/pnas.83.22.8703;
RA   Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F.;
RT   "Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI
RT   129/J mice is a parasite glutathione S-transferase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:8703-8707(1986).
RN   [2]
RP   SEQUENCE REVISION.
RA   Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F.;
RL   Proc. Natl. Acad. Sci. U.S.A. 84:6541-6541(1987).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-15.
RX   PubMed=3278228; DOI=10.1016/0166-6851(88)90044-8;
RA   Smith D.B., Rubira M.R., Simpson R.J., Davern K.M., Tiu W.U., Board P.G.,
RA   Mitchell G.F.;
RT   "Expression of an enzymatically active parasite molecule in Escherichia
RT   coli: Schistosoma japonicum glutathione S-transferase.";
RL   Mol. Biochem. Parasitol. 27:249-256(1988).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RX   PubMed=7538846; DOI=10.1002/pro.5560031209;
RA   Lim K., Ho J.X., Keeling K., Gilliland G.L., Ji X., Ruker F., Carter D.C.;
RT   "Three-dimensional structure of Schistosoma japonicum glutathione S-
RT   transferase fused with a six-amino acid conserved neutralizing epitope of
RT   gp41 from HIV.";
RL   Protein Sci. 3:2233-2244(1994).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITOR
RP   PRAZIQUANTEL.
RX   PubMed=7853399; DOI=10.1006/jmbi.1994.0061;
RA   McTigue M.A., Williams D.R., Tainer J.A.;
RT   "Crystal structures of a schistosomal drug and vaccine target: glutathione
RT   S-transferase from Schistosoma japonica and its complex with the leading
RT   antischistosomal drug praziquantel.";
RL   J. Mol. Biol. 246:21-27(1995).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE
RP   ANALOGS.
RX   PubMed=12596270; DOI=10.1002/prot.10345;
RA   Cardoso R.M., Daniels D.S., Bruns C.M., Tainer J.A.;
RT   "Characterization of the electrophile binding site and substrate binding
RT   mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum.";
RL   Proteins 51:137-146(2003).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-214.
RX   PubMed=19177365; DOI=10.1002/pro.23;
RA   Sagermann M., Chapleau R.R., DeLorimier E., Lei M.;
RT   "Using affinity chromatography to engineer and characterize pH-dependent
RT   protein switches.";
RL   Protein Sci. 18:217-228(2009).
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. {ECO:0000269|PubMed:7853399}.
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; M14654; AAB59203.1; -; mRNA.
DR   PIR; A61514; A61514.
DR   PDB; 1B8X; X-ray; 2.70 A; A=2-218.
DR   PDB; 1BG5; X-ray; 2.60 A; A=1-218.
DR   PDB; 1DUG; X-ray; 1.80 A; A/B=2-218.
DR   PDB; 1GNE; X-ray; 2.50 A; A=2-218.
DR   PDB; 1GTA; X-ray; 2.40 A; A=1-218.
DR   PDB; 1GTB; X-ray; 2.60 A; A=1-218.
DR   PDB; 1M99; X-ray; 2.30 A; A=1-218.
DR   PDB; 1M9A; X-ray; 2.10 A; A=1-218.
DR   PDB; 1M9B; X-ray; 2.60 A; A=1-218.
DR   PDB; 1U87; X-ray; 3.50 A; A=1-218.
DR   PDB; 1U88; X-ray; 3.50 A; A/B=1-218.
DR   PDB; 1UA5; X-ray; 2.50 A; A=1-218.
DR   PDB; 1Y6E; X-ray; 3.00 A; A/B=2-218.
DR   PDB; 3CRT; X-ray; 1.90 A; A=1-214.
DR   PDB; 3CRU; X-ray; 2.30 A; A=1-214.
DR   PDB; 3D0Z; X-ray; 2.50 A; A=1-214.
DR   PDB; 3QMZ; X-ray; 6.00 A; S/T=2-218.
DR   PDB; 4AI6; X-ray; 3.40 A; A/B=2-218.
DR   PDB; 4AKG; X-ray; 3.30 A; A/B=2-218.
DR   PDB; 4AKH; X-ray; 3.60 A; A/B=2-218.
DR   PDB; 4AKI; X-ray; 3.70 A; A/B=2-218.
DR   PDB; 4ECB; X-ray; 2.20 A; A/B=1-218.
DR   PDB; 4ECC; X-ray; 2.20 A; A=1-215.
DR   PDB; 4WR4; X-ray; 1.60 A; A=2-218.
DR   PDB; 4WR5; X-ray; 1.93 A; A=2-218.
DR   PDB; 5GZZ; X-ray; 2.39 A; B/C/D/E/F/G=1-218.
DR   PDB; 6JI6; X-ray; 1.50 A; A=1-218.
DR   PDB; 6N8U; X-ray; 1.96 A; A/B=1-218.
DR   PDB; 6RWD; X-ray; 1.53 A; A/B=1-218.
DR   PDB; 7AL7; X-ray; 1.80 A; B=2-218.
DR   PDB; 7ESG; X-ray; 2.53 A; A=1-218.
DR   PDB; 7NT8; X-ray; 2.22 A; A/B=1-218.
DR   PDB; 7XQK; X-ray; 2.25 A; A=1-218.
DR   PDB; 8DHB; EM; 3.53 A; H=2-218.
DR   PDB; 8FW5; EM; 3.08 A; F=1-218.
DR   PDB; 8GYD; X-ray; 1.70 A; A/B=1-218.
DR   PDB; 8H4R; X-ray; 2.75 A; A=1-218.
DR   PDB; 8JHU; EM; 3.10 A; A=1-218.
DR   PDB; 8SEN; EM; 3.49 A; E/F/G/H=1-218.
DR   PDB; 8SEO; EM; 3.92 A; E/F/G/H=1-218.
DR   PDB; 8SEP; EM; 3.57 A; E/F/G/H=1-218.
DR   PDB; 8SEQ; EM; 3.40 A; E/F/G/H=1-218.
DR   PDB; 8SER; EM; 3.42 A; E/F/G/H=1-218.
DR   PDB; 8SES; EM; 3.98 A; E/F/G/H=1-218.
DR   PDB; 8SET; EM; 3.42 A; E/F/G/H=1-218.
DR   PDBsum; 1B8X; -.
DR   PDBsum; 1BG5; -.
DR   PDBsum; 1DUG; -.
DR   PDBsum; 1GNE; -.
DR   PDBsum; 1GTA; -.
DR   PDBsum; 1GTB; -.
DR   PDBsum; 1M99; -.
DR   PDBsum; 1M9A; -.
DR   PDBsum; 1M9B; -.
DR   PDBsum; 1U87; -.
DR   PDBsum; 1U88; -.
DR   PDBsum; 1UA5; -.
DR   PDBsum; 1Y6E; -.
DR   PDBsum; 3CRT; -.
DR   PDBsum; 3CRU; -.
DR   PDBsum; 3D0Z; -.
DR   PDBsum; 3QMZ; -.
DR   PDBsum; 4AI6; -.
DR   PDBsum; 4AKG; -.
DR   PDBsum; 4AKH; -.
DR   PDBsum; 4AKI; -.
DR   PDBsum; 4ECB; -.
DR   PDBsum; 4ECC; -.
DR   PDBsum; 4WR4; -.
DR   PDBsum; 4WR5; -.
DR   PDBsum; 5GZZ; -.
DR   PDBsum; 6JI6; -.
DR   PDBsum; 6N8U; -.
DR   PDBsum; 6RWD; -.
DR   PDBsum; 7AL7; -.
DR   PDBsum; 7ESG; -.
DR   PDBsum; 7NT8; -.
DR   PDBsum; 7XQK; -.
DR   PDBsum; 8DHB; -.
DR   PDBsum; 8FW5; -.
DR   PDBsum; 8GYD; -.
DR   PDBsum; 8H4R; -.
DR   PDBsum; 8JHU; -.
DR   PDBsum; 8SEN; -.
DR   PDBsum; 8SEO; -.
DR   PDBsum; 8SEP; -.
DR   PDBsum; 8SEQ; -.
DR   PDBsum; 8SER; -.
DR   PDBsum; 8SES; -.
DR   PDBsum; 8SET; -.
DR   AlphaFoldDB; P08515; -.
DR   SASBDB; P08515; -.
DR   SMR; P08515; -.
DR   DrugCentral; P08515; -.
DR   ABCD; P08515; 23 sequenced antibodies.
DR   BRENDA; 2.5.1.18; 5607.
DR   SABIO-RK; P08515; -.
DR   EvolutionaryTrace; P08515; -.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03209; GST_C_Mu; 1.
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; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF222; GLUTATHIONE S-TRANSFERASE 2-RELATED; 1.
DR   Pfam; PF14497; GST_C_3; 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   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3278228"
FT   CHAIN           2..218
FT                   /note="Glutathione S-transferase class-mu 26 kDa isozyme"
FT                   /id="PRO_0000185805"
FT   DOMAIN          2..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:0000269|PubMed:7538846,
FT                   ECO:0000305|PubMed:12596270"
FT   BINDING         41..45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:7538846,
FT                   ECO:0000305|PubMed:12596270"
FT   BINDING         54..55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:7538846,
FT                   ECO:0000305|PubMed:12596270"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:7538846,
FT                   ECO:0000305|PubMed:12596270"
FT   BINDING         111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..11
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   HELIX           15..23
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   HELIX           25..28
FT                   /evidence="ECO:0007829|PDB:7ESG"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:6N8U"
FT   HELIX           38..44
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:4WR5"
FT   STRAND          55..60
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   HELIX           68..78
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   STRAND          81..84
FT                   /evidence="ECO:0007829|PDB:7ESG"
FT   HELIX           86..110
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:4AKG"
FT   HELIX           115..136
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   TURN            137..139
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   HELIX           140..143
FT                   /evidence="ECO:0007829|PDB:7ESG"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   HELIX           150..165
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   TURN            167..172
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   HELIX           174..185
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   HELIX           187..194
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   STRAND          195..197
FT                   /evidence="ECO:0007829|PDB:1GTA"
FT   HELIX           200..203
FT                   /evidence="ECO:0007829|PDB:7ESG"
FT   STRAND          209..211
FT                   /evidence="ECO:0007829|PDB:6JI6"
FT   STRAND          213..215
FT                   /evidence="ECO:0007829|PDB:6RWD"
SQ   SEQUENCE   218 AA;  25499 MW;  5E2AC418BD0EF13F CRC64;
     MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID
     GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV
     DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK
     KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPK
//