Glutathione synthetase (P04425)

Identification
Name:Glutathione synthetase
Synonyms:
  • GSH synthetase
  • GSH-S
  • GSHase
  • Glutathione synthase
Gene Name:gshB
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0gamma-Glutamylcysteine + 1.0Glycine ↔ 1.0ADP + 1.0Glutathione + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0gamma-Glutamylcysteine + 1.0Glycine ↔ 1.0ADP + 1.0Phosphate + 1.0Glutathione
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Adenosine diphosphate+1.0Thumb+1.0Thumb
1.0gamma-Glutamylcysteine + 1.0Glycine + 1.0Adenosine triphosphate → 1.0Hydrogen ion + 1.0Phosphate + 1.0Adenosine diphosphate + 1.0Glutathione + 1.0ADP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0gamma-Glutamylcysteine + 1.0Glycine ↔ 1.0ADP + 1.0Glutathione + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0gamma-Glutamylcysteine + 1.0Glycine → 1.0ADP + 1.0Inorganic phosphate + 1.0Glutathione
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01049gamma-GlutamylcysteineMetaboCard
ECMDB00125GlutathioneMetaboCard
ECMDB00123GlycineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
GO Classification:
Function
acid-amino acid ligase activity
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
glutathione synthase activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
nucleoside binding
purine nucleoside binding
Process
cellular metabolic process
glutathione biosynthetic process
glutathione metabolic process
metabolic process
peptide metabolic process
Gene Properties
Blattner:b2947
Gene OrientationClockwise
Centisome Percentage:66.60
Left Sequence End3089900
Right Sequence End3090850
Gene Sequence:
>951 bp
ATGCAGATCCTGTTGGCCAACCCGCGTGGTTTTTGTGCCGGGGTAGACCGCGCTATCAGC
ATTGTTGAAAACGCGCTGGCCATTTACGGCGCACCGATATATGTCCGTCACGAAGTGGTA
CATAACCGCTATGTGGTCGATAGCTTGCGTGAGCGTGGGGCTATCTTTATTGAGCAGATT
AGCGAAGTACCGGACGGCGCGATCCTGATTTTCTCCGCACACGGTGTTTCTCAGGCGGTA
CGTAACGAAGCAAAAAGTCGCGATTTGACGGTGTTTGATGCCACCTGTCCGCTGGTGACC
AAAGTGCATATGGAAGTCGCCCGCGCCAGTCGCCGTGGCGAAGAATCTATTCTCATCGGT
CACGCCGGGCACCCGGAAGTGGAAGGGACAATGGGCCAGTACAGTAACCCGGAAGGGGGA
ATGTATCTGGTCGAATCGCCGGACGATGTGTGGAAACTGACGGTCAAAAACGAAGAGAAG
CTCTCCTTTATGACCCAGACCACGCTGTCGGTGGATGACACGTCTGATGTGATCGACGCG
CTGCGTAAACGCTTCCCGAAAATTGTCGGTCCGCGCAAAGATGACATCTGCTACGCCACG
ACTAACCGTCAGGAAGCGGTACGCGCCCTGGCAGAACAGGCGGAAGTTGTGTTGGTGGTC
GGTTCGAAAAACTCCTCCAACTCCAACCGTCTGGCGGAGCTGGCCCAGCGTATGGGCAAA
CGCGCGTTTTTGATTGACGATGCGAAAGACATCCAGGAAGAGTGGGTGAAAGAGGTTAAA
TGCGTCGGCGTGACTGCGGGCGCATCGGCTCCGGATATTCTGGTGCAGAATGTGGTGGCA
CGTTTGCAGCAGCTGGGCGGTGGTGAAGCCATTCCGCTGGAAGGCCGTGAAGAAAACATT
GTTTTCGAAGTGCCGAAAGAGCTGCGTGTCGATATTCGTGAAGTCGATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:316
Protein Molecular Weight:35561
Protein Theoretical pI:5
PDB File:2GLT
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glutathione synthetase
MIKLGIVMDPIANINIKKDSSFAMLLEAQRRGYELHYMEMGDLYLINGEARAHTRTLNVK
QNYEEWFSFVGEQDLPLADLDVILMRKDPPFDTEFIYATYILERAEEKGTLIVNKPQSLR
DCNEKLFTAWFSDLTPETLVTRNKAQLKAFWEKHSDIILKPLDGMGGASIFRVKEGDPNL
GVIAETLTEHGTRYCMAQNYLPAIKDGDKRVLVVDGEPVPYCLARIPQGGETRGNLAAGG
RGEPRPLTESDWKIARQIGPTLKEKGLIFVGLDIIGDRLTEINVTSPTCIREIEAEFPVS
ITGMLMDAIEARLQQQ
References
External Links:
ResourceLink
Uniprot ID:P04425
Uniprot Name:GSHB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321911
PDB ID:2GLT
Ecogene ID:EG10419
Ecocyc:EG10419
ColiBase:b2947
Kegg Gene:b2947
EchoBASE ID:EB0414
CCDB:GSHB_ECOLI
BacMap:16130848
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Gushima, H., Yasuda, S., Soeda, E., Yokota, M., Kondo, M., Kimura, A. (1984). "Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II." Nucleic Acids Res 12:9299-9307. Pubmed: 6393055
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kato, H., Tanaka, T., Nishioka, T., Kimura, A., Oda, J. (1988). "Role of cysteine residues in glutathione synthetase from Escherichia coli B. Chemical modification and oligonucleotide site-directed mutagenesis." J Biol Chem 263:11646-11651. Pubmed: 3042775
  • Matsuda, K., Mizuguchi, K., Nishioka, T., Kato, H., Go, N., Oda, J. (1996). "Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins." Protein Eng 9:1083-1092. Pubmed: 9010922
  • Tanaka, T., Kato, H., Nishioka, T., Oda, J. (1992). "Mutational and proteolytic studies on a flexible loop in glutathione synthetase from Escherichia coli B: the loop and arginine 233 are critical for the catalytic reaction." Biochemistry 31:2259-2265. Pubmed: 1540581
  • Tanaka, T., Yamaguchi, H., Kato, H., Nishioka, T., Katsube, Y., Oda, J. (1993). "Flexibility impaired by mutations revealed the multifunctional roles of the loop in glutathione synthetase." Biochemistry 32:12398-12404. Pubmed: 8241129
  • Yamaguchi, H., Kato, H., Hata, Y., Nishioka, T., Kimura, A., Oda, J., Katsube, Y. (1993). "Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 A resolution." J Mol Biol 229:1083-1100. Pubmed: 8445637