Glutathione S-transferase GstA
Details
- Name
- Glutathione S-transferase GstA
- Kind
- protein
- Synonyms
- 2.5.1.18
- gst
- GST B1-1
- Gene Name
- gstA
- UniProtKB Entry
- P0A9D2Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0019227|Glutathione S-transferase GstA MKLFYKPGACSLASHITLRESGKDFTLVSVDLMKKRLENGDDYFAVNPKGQVPALLLDDG TLLTEGVAIMQYLADSVPDRQLLAPVNSISRYKTIEWLNYIATELHKGFTPLFRPDTPEE YKPTVRAQLEKKLQYVNEALKDEHWICGQRFTIADAYLFTVLRWAYAVKLNLEGLEHIAA FMQRMAERPEVQDALSAEGLK
- Number of residues
- 201
- Molecular Weight
- 22868.14
- Theoretical pI
- 6.13
- GO Classification
- Functionsglutathione transferase activityProcessesglutathione metabolic process / xenobiotic catabolic processComponentscytoplasm
- General Function
- Catalyzes the conjugation of reduced glutathione (GSH) to a wide number of exogenous and endogenous hydrophobic electrophiles. Shows activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid. Also possesses thiol:disulfide oxidoreductase activity, using GSH to reduce bis-(2-hydroxyethyl) disulfide (HEDS). Has a low level of glutathione-dependent peroxidase activity toward cumene hydroperoxide. Is important for defense against oxidative stress, probably via its peroxidase activity.
- Specific Function
- glutathione transferase activity
- Pfam Domain Function
- Not Available
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0019228|Glutathione S-transferase GstA (gstA) ATGAAATTGTTCTACAAACCGGGTGCCTGCTCTCTCGCTTCCCATATCACCCTGCGTGAG AGCGGAAAGGATTTTACCCTCGTCAGTGTGGATTTAATGAAAAAACGTCTCGAAAACGGT GACGATTACTTTGCCGTTAACCCTAAGGGGCAGGTGCCTGCATTGCTGCTGGATGACGGT ACTTTGCTGACGGAAGGCGTAGCGATTATGCAGTATCTTGCCGACAGCGTCCCCGACCGC CAGTTGCTGGCACCGGTAAACAGTATTTCCCGCTATAAAACCATCGAATGGCTGAATTAC ATCGCCACCGAGCTGCATAAAGGTTTCACACCTCTGTTTCGCCCTGATACACCGGAAGAG TACAAACCGACAGTTCGCGCGCAGCTGGAGAAGAAGCTGCAATATGTGAACGAGGCACTG AAGGATGAGCACTGGATCTGCGGGCAAAGATTTACAATTGCTGATGCCTATCTGTTTACG GTTCTGCGCTGGGCATACGCGGTGAAACTGAATCTGGAAGGGTTAGAGCACATTGCAGCA TTTATGCAACGTATGGCTGAACGTCCGGAAGTACAAGACGCGCTGTCAGCGGAAGGCTTA AAGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A9D2 UniProtKB Entry Name GSTA_ECOLI GenBank Gene ID D38497 PDB ID(s) 1A0F, 1N2A KEGG ID ecj:JW1627 NCBI Gene ID 945758 - General References
- Nishida M, Kong KH, Inoue H, Takahashi K: Molecular cloning and site-directed mutagenesis of glutathione S-transferase from Escherichia coli. The conserved tyrosyl residue near the N terminus is not essential for catalysis. J Biol Chem. 1994 Dec 23;269(51):32536-41. [Article]
- Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Arca P, Garcia P, Hardisson C, Suarez JE: Purification and study of a bacterial glutathione S-transferase. FEBS Lett. 1990 Apr 9;263(1):77-9. [Article]
- Kanai T, Takahashi K, Inoue H: Three distinct-type glutathione S-transferases from Escherichia coli important for defense against oxidative stress. J Biochem. 2006 Nov;140(5):703-11. Epub 2006 Oct 3. [Article]
- Wang XY, Zhang ZR, Perrett S: Characterization of the activity and folding of the glutathione transferase from Escherichia coli and the roles of residues Cys(10) and His(106). Biochem J. 2009 Jan 1;417(1):55-64. doi: 10.1042/BJ20071702. [Article]
- Nishida M, Harada S, Noguchi S, Satow Y, Inoue H, Takahashi K: Three-dimensional structure of Escherichia coli glutathione S-transferase complexed with glutathione sulfonate: catalytic roles of Cys10 and His106. J Mol Biol. 1998 Aug 7;281(1):135-47. [Article]
- Rife CL, Parsons JF, Xiao G, Gilliland GL, Armstrong RN: Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli. Proteins. 2003 Dec 1;53(4):777-82. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Glutathione sulfonic acid experimental unknown target Details