GST28_SCHHA
ID GST28_SCHHA Reviewed; 211 AA.
AC P30114;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Glutathione S-transferase class-mu 28 kDa isozyme;
DE Short=GST 28;
DE EC=2.5.1.18;
DE AltName: Full=Sh28GST;
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]
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).
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};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12939136}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; M87800; AAA29893.1; -; Genomic_DNA.
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 PDBsum; 1OE7; -.
DR PDBsum; 1OE8; -.
DR AlphaFoldDB; P30114; -.
DR SMR; P30114; -.
DR BRENDA; 2.5.1.18; 7965.
DR EvolutionaryTrace; P30114; -.
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; 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 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_0000185813"
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:12939136"
FT BINDING 16
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:12939136"
FT BINDING 41..45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:12939136"
FT BINDING 53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:12939136"
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:12939136"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:1OE8"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:1OE8"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1OE8"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1OE8"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1OE8"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1OE8"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1OE7"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1OE8"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1OE8"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:1OE8"
FT HELIX 89..110
FT /evidence="ECO:0007829|PDB:1OE8"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:1OE8"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:1OE8"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:1OE8"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1OE8"
FT HELIX 158..173
FT /evidence="ECO:0007829|PDB:1OE8"
FT TURN 175..180
FT /evidence="ECO:0007829|PDB:1OE8"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:1OE8"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:1OE8"
SQ SEQUENCE 211 AA; 23960 MW; 954B2B60AA22E2C8 CRC64;
MTGDHIKVIY FNGRGRAESI RMTLVAAGVN YEDERISFQD WPKIKPTIPG GRLPAVKITD
NHGHVKWMLE SLAIARYMAK KHHMMGETDE EYYNVEKLIG QVEDLEHEYH KTLMKPEEEK
QKITKEILNG KVPVLLDIIC ESLKASTGKL AVGDKVTLAD LVLIAVIDHV TDLDKEFLTG
KYPEIHKHRE NLLASSPRLA KYLSDRAATP F
