ID   Q9U795_MUSDO            Unreviewed;       222 AA.
AC   Q9U795;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=Glutathione s-transferase 6B {ECO:0000313|EMBL:AAD54938.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:AAD54938.1};
GN   Name=GST-6B {ECO:0000313|EMBL:AAD54938.1};
OS   Musca domestica (House fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Musca.
OX   NCBI_TaxID=7370 {ECO:0000313|EMBL:AAD54938.1};
RN   [1] {ECO:0000313|EMBL:AAD54938.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Cornell-HR {ECO:0000313|EMBL:AAD54938.1};
RA   Wei S.H., Syvanen M.;
RT   "Glutathione S-transferase associated with OP-insecticide resistance in the
RT   housefly Musca domestica.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:3VWX}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RX   PubMed=23268341; DOI=10.1016/j.bbrc.2012.12.077;
RA   Nakamura C., Yajima S., Miyamoto T., Sue M.;
RT   "Structural analysis of an epsilon-class glutathione transferase from
RT   housefly, Musca domestica.";
RL   Biochem. Biophys. Res. Commun. 430:1206-1211(2013).
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DR   EMBL; AF147206; AAD54938.1; -; mRNA.
DR   PDB; 3VWX; X-ray; 1.80 A; A/B/C/D=1-222.
DR   PDBsum; 3VWX; -.
DR   AlphaFoldDB; Q9U795; -.
DR   SMR; Q9U795; -.
DR   VEuPathDB; VectorBase:MDOA009496; -.
DR   BRENDA; 2.5.1.18; 3486.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03177; GST_C_Delta_Epsilon; 1.
DR   CDD; cd03045; GST_N_Delta_Epsilon; 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; PTHR43969:SF4; FI01423P-RELATED; 1.
DR   PANTHER; PTHR43969; GLUTATHIONE S TRANSFERASE D10, ISOFORM A-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01153; Main.4:_Theta-like; 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 {ECO:0007829|PDB:3VWX};
KW   Transferase {ECO:0000313|EMBL:AAD54938.1}.
FT   DOMAIN          2..83
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          89..213
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   BINDING         12
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0007829|PDB:3VWX"
FT   BINDING         41
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0007829|PDB:3VWX"
FT   BINDING         53
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0007829|PDB:3VWX"
FT   BINDING         55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0007829|PDB:3VWX"
FT   BINDING         68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0007829|PDB:3VWX"
FT   BINDING         113
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0007829|PDB:3VWX"
SQ   SEQUENCE   222 AA;  25025 MW;  B1740ABEFD4151FC CRC64;
     MGKLVLYGID PSPPVRACLL TLKALNLPFE YKVVNLFAKE HLSEEYLKKN PQHTVPTLEE
     DGHLIWDSHP IMAYLVSKYG KDDSLYPKDL LKRAVVDQRM YFEAGVLFQG GLRNITAPLF
     FRNQTQIPQH QIDSIVESYG FLESFLKNNK YMAGDHLTIA DFSIVTSVTS LVAFAEIDQS
     KFPKLSAWLK SLQSLPFYEE ANGAGAKQLV AMVKSKNLTI VP
//