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GSTT1_MANSE
ID   GSTT1_MANSE             Reviewed;         217 AA.
AC   P46430;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Glutathione S-transferase 1;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-theta;
GN   Name=GST1;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Midgut;
RX   PubMed=7742833; DOI=10.1016/0965-1748(94)00083-b;
RA   Snyder M.J., Walding J.K., Feyereisen R.;
RT   "Glutathione S-transferases from larval Manduca sexta midgut: sequence of
RT   two cDNAs and enzyme induction.";
RL   Insect Biochem. Mol. Biol. 25:455-465(1995).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
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   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000305}.
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DR   EMBL; L32091; AAA92880.1; -; mRNA.
DR   AlphaFoldDB; P46430; -.
DR   SMR; P46430; -.
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; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 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   2: Evidence at transcript level;
KW   Transferase.
FT   CHAIN           1..217
FT                   /note="Glutathione S-transferase 1"
FT                   /id="PRO_0000185964"
FT   DOMAIN          1..83
FT                   /note="GST N-terminal"
FT   DOMAIN          89..211
FT                   /note="GST C-terminal"
FT   BINDING         11
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         53..55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..69
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   217 AA;  24431 MW;  630281A2975E56C0 CRC64;
     MVMTLYKLDA SPPARAVMMV IEALKIPDVE YIDVNLLEGS HLSEEFTKMN PQHTVPLLKD
     DDFLVWDSHA IAGYLVSKYG ADDSLYPTDP KKRAIVDQRL HFDSGILFPA LRGSLEPVIF
     WGETAFRPEC LEKVRKGYDF AEKFLTSTWM AGEEFTVADI CCVASISTMN DIIVPIDENT
     YPKLSAWLER CSQLDVYKKK NAPGNDLCKD LVASKLS
 
 
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