ID GST28_SCHHA Reviewed; 211 AA. AC P30113; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 27-MAR-2024, entry version 109. DE RecName: Full=Glutathione S-transferase class-mu 28 kDa isozyme; DE Short=GST 28; DE EC=2.5.1.18 {ECO:0000269|PubMed:12939136, ECO:0000269|PubMed:16777141}; DE AltName: Full=Sb28GST; OS Schistosoma haematobium (Blood fluke). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda; OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma. OX NCBI_TaxID=6185; 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] {ECO:0007744|PDB:1OE7, ECO:0007744|PDB:1OE8} RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, RP FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY. RX PubMed=12939136; DOI=10.1021/bi034449r; RA Johnson K.A., Angelucci F., Bellelli A., Herve M., Fontaine J., RA Tsernoglou D., Capron A., Trottein F., Brunori M.; RT "Crystal structure of the 28 kDa glutathione S-transferase from Schistosoma RT haematobium."; RL Biochemistry 42:10084-10094(2003). RN [3] {ECO:0007744|PDB:2C80, ECO:0007744|PDB:2C8U, ECO:0007744|PDB:2CA8, ECO:0007744|PDB:2CAI, ECO:0007744|PDB:2CAQ, ECO:0007744|PDB:2F8F} 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 {ECO:0000269|PubMed:12939136}. 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 {ECO:0000269|PubMed:12939136}. 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:12939136, ECO:0000269|PubMed:16777141}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12939136, CC 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M87799; AAA29892.1; ALT_INIT; Genomic_DNA. DR RefSeq; XP_012797862.1; XM_012942408.1. DR PDB; 1OE7; X-ray; 1.80 A; A/B=1-211. DR PDB; 1OE8; X-ray; 1.65 A; A/B=1-211. 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; 1OE7; -. DR PDBsum; 1OE8; -. 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 GeneID; 24593871; -. DR EvolutionaryTrace; P30113; -. 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 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 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:12939136, FT ECO:0000269|PubMed:16777141, ECO:0007744|PDB:1OE7, FT ECO:0007744|PDB:2C80, ECO:0007744|PDB:2CA8" FT BINDING 16 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:12939136, FT ECO:0000269|PubMed:16777141, ECO:0007744|PDB:1OE7, FT ECO:0007744|PDB:2C80, ECO:0007744|PDB:2CA8, FT ECO:0007744|PDB:2CAQ" FT BINDING 41 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:12939136, FT ECO:0000269|PubMed:16777141, ECO:0007744|PDB:1OE7, FT ECO:0007744|PDB:1OE8, ECO:0007744|PDB:2C80, FT ECO:0007744|PDB:2CA8, ECO:0007744|PDB:2CAQ, FT ECO:0007744|PDB:2F8F" FT BINDING 45 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:12939136, FT ECO:0000269|PubMed:16777141, ECO:0007744|PDB:1OE7, FT ECO:0007744|PDB:1OE8, ECO:0007744|PDB:2C80, FT ECO:0007744|PDB:2CA8, ECO:0007744|PDB:2CAQ, FT ECO:0007744|PDB:2F8F" FT BINDING 53 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:12939136, FT ECO:0000269|PubMed:16777141, ECO:0007744|PDB:1OE7, FT ECO:0007744|PDB:1OE8, ECO:0007744|PDB:2C80, FT ECO:0007744|PDB:2CA8, ECO:0007744|PDB:2CAQ, FT ECO:0007744|PDB:2F8F" FT BINDING 70 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:12939136, FT ECO:0000269|PubMed:16777141, ECO:0007744|PDB:1OE7, FT ECO:0007744|PDB:1OE8, ECO:0007744|PDB:2C80, FT ECO:0007744|PDB:2CA8, ECO:0007744|PDB:2CAQ, FT ECO:0007744|PDB:2F8F" FT BINDING 71 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:12939136, FT ECO:0000269|PubMed:16777141, ECO:0007744|PDB:1OE7, FT ECO:0007744|PDB:1OE8, ECO:0007744|PDB:2C80, FT ECO:0007744|PDB:2CA8, ECO:0007744|PDB:2CAQ, FT ECO:0007744|PDB:2F8F" FT BINDING 104 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:12939136, FT ECO:0000269|PubMed:16777141, ECO:0007744|PDB:1OE7, FT ECO:0007744|PDB:2C80, ECO:0007744|PDB:2F8F" 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 //