GST28_SCHBO
ID GST28_SCHBO Reviewed; 211 AA.
AC P30113;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Glutathione S-transferase class-mu 28 kDa isozyme;
DE Short=GST 28;
DE EC=2.5.1.18 {ECO:0000269|PubMed:16777141};
DE AltName: Full=Sb28GST;
OS Schistosoma bovis (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6184;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1518533; DOI=10.1016/0166-6851(92)90095-2;
RA Trottein F., Goding G., Sellin B., Gorillot I., Samaio M., Lecocq J.-P.,
RA Capron A.;
RT "Inter-species variation of schistosome 28-kDa glutathione S-
RT transferases.";
RL Mol. Biochem. Parasitol. 54:63-72(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT,
RP MUTAGENESIS OF TYR-10 AND ARG-21, AND CATALYTIC ACTIVITY.
RX PubMed=16777141; DOI=10.1016/j.jmb.2006.05.040;
RA Baiocco P., Gourlay L.J., Angelucci F., Fontaine J., Herve M., Miele A.E.,
RA Trottein F., Brunori M., Bellelli A.;
RT "Probing the mechanism of GSH activation in Schistosoma haematobium
RT glutathione-S-transferase by site-directed mutagenesis and X-ray
RT crystallography.";
RL J. Mol. Biol. 360:678-689(2006).
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 Evidence={ECO:0000269|PubMed:16777141};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16777141}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA29892.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M87799; AAA29892.1; ALT_INIT; Genomic_DNA.
DR PDB; 2C80; X-ray; 2.30 A; A/B=1-211.
DR PDB; 2C8U; X-ray; 2.00 A; A/B=1-211.
DR PDB; 2CA8; X-ray; 2.49 A; A=1-211.
DR PDB; 2CAI; X-ray; 2.26 A; A/B=1-211.
DR PDB; 2CAQ; X-ray; 2.00 A; A=1-211.
DR PDB; 2F8F; X-ray; 2.10 A; A/B=1-211.
DR PDBsum; 2C80; -.
DR PDBsum; 2C8U; -.
DR PDBsum; 2CA8; -.
DR PDBsum; 2CAI; -.
DR PDBsum; 2CAQ; -.
DR PDBsum; 2F8F; -.
DR AlphaFoldDB; P30113; -.
DR SMR; P30113; -.
DR EvolutionaryTrace; P30113; -.
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 1: Evidence at protein level;
KW 3D-structure; Transferase.
FT CHAIN 1..211
FT /note="Glutathione S-transferase class-mu 28 kDa isozyme"
FT /id="PRO_0000185812"
FT DOMAIN 4..86
FT /note="GST N-terminal"
FT DOMAIN 88..211
FT /note="GST C-terminal"
FT BINDING 10..11
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 10
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16777141"
FT BINDING 16
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16777141"
FT BINDING 41..45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16777141"
FT BINDING 53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16777141"
FT BINDING 55..56
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 70..71
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:16777141"
FT MUTAGEN 10
FT /note="Y->F: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:16777141"
FT MUTAGEN 21
FT /note="R->L: Reduces catalytic activity 12-fold."
FT /evidence="ECO:0000269|PubMed:16777141"
FT MUTAGEN 21
FT /note="R->Q: Reduces catalytic activity 120-fold."
FT /evidence="ECO:0000269|PubMed:16777141"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:2C8U"
FT TURN 13..17
FT /evidence="ECO:0007829|PDB:2C8U"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:2C8U"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2C8U"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:2C8U"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:2C8U"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2C8U"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:2C8U"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2C8U"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:2C8U"
FT HELIX 89..110
FT /evidence="ECO:0007829|PDB:2C8U"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:2C8U"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:2C8U"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:2C8U"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:2C8U"
FT HELIX 158..173
FT /evidence="ECO:0007829|PDB:2C8U"
FT TURN 175..180
FT /evidence="ECO:0007829|PDB:2C8U"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:2C8U"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:2C8U"
SQ SEQUENCE 211 AA; 23898 MW; 9B9F1358710D3C76 CRC64;
MTGDHIKVIY FNGRGRAESI RMTLVAAGVN YEDERISFQD WPKIKPTIPG GRLPAVKITD
NHGHVKWMVE SLAIARYMAK KHHMMGGTEE EYYNVEKLIG QAEDLEHEYY KTLMKPEEEK
QKIIKEILNG KVPVLLDIIC ESLKASTGKL AVGDKVTLAD LVLIAVIDHV TDLDKEFLTG
KYPEIHKHRE NLLASSPRLA KYLSDRAATP F
