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   04-NOV-2008, entry version 61.
DE   RecName: Full=Glutathione S-transferase class-mu 28 kDa isozyme;
DE            Short=GST 28;
DE            EC=2.5.1.18;
DE   AltName: Full=Sb28GST;
OS   Schistosoma bovis (Blood fluke).
OC   Eukaryota; Metazoa; Platyhelminthes; Trematoda; Digenea; Strigeidida;
OC   Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6184;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92389991; PubMed=1518533; DOI=10.1016/0166-6851(92)90095-2;
RA   Trottein F., Goding G., Sellin B., Gorillot I., Samaio M.,
RA   Lecocq J.-P., 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).
RX   PubMed=16777141; DOI=10.1016/j.jmb.2006.05.040;
RA   Baiocco P., Gourlay L.J., Angelucci F., Fontaine J., Herve M.,
RA   Miele A.E., 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
CC       parasite detoxification system. Other functions are also suspected
CC       including a role in increasing the solubility of haematin in the
CC       parasite gut.
CC   -!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Mu family.
CC   -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC   -!- SIMILARITY: Contains 1 GST N-terminal domain.
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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   DrugBank; DB00143; Glutathione.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:EC.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR004045; GST_N.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 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       Glutathione S-transferase class-mu 28 kDa
FT                                isozyme.
FT                                /FTId=PRO_0000185812.
FT   DOMAIN        4     86       GST N-terminal.
FT   DOMAIN       88    211       GST C-terminal.
FT   ACT_SITE     10     10
FT   STRAND        5     11
FT   TURN         13     17
FT   HELIX        18     27
FT   STRAND       32     35
FT   TURN         38     40
FT   TURN         42     44
FT   HELIX        45     47
FT   STRAND       53     59
FT   STRAND       65     69
FT   HELIX        71     81
FT   HELIX        89    110
FT   HELIX       117    129
FT   HELIX       131    144
FT   STRAND      147    152
FT   HELIX       158    173
FT   HELIX       183    195
FT   HELIX       197    203
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
//