Glutathione reductase (P06715)

Identification
Name:Glutathione reductase
Synonyms:
  • GR
  • GRase
Gene Name:gor
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity
Specific Function:Maintains high levels of reduced glutathione in the cytosol
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 2.0Thumb+1.0Thumb
1.0Glutathione disulfide + 1.0Hydrogen ion + 1.0NADPH ↔ 2.0Glutathione + 1.0NADP
ReactionCard
2.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
2.0Glutathione + 1.0NAD ↔ 1.0Glutathione disulfide + 1.0NADH + 1.0Hydrogen ion
ReactionCard
2.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
2.0Glutathione + 1.0NADP ↔ 1.0Glutathione disulfide + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
SMPDB Reactions:
1.0Oxidized glutathione+1.0Thumb+1.0NADPH+1.0Thumb+1.0Thumb → 1.0Thumb+2.0Thumb
1.0Oxidized glutathione + 1.0Hydrogen ion + 1.0NADPH + 1.0Glutathione disulfide + 1.0NADPH → 1.0NADP + 2.0Glutathione
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 2.0Thumb+1.0Thumb
1.0Glutathione disulfide + 1.0Hydrogen ion + 1.0NADPH ↔ 2.0Glutathione + 1.0NADP
ReactionCard
Complex Reactions:
2.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
2.0Glutathione + 1.0NADP → 1.0Glutathione disulfide + 1.0NADPH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00125GlutathioneMetaboCard
ECMDB21221Glutathione disulfideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
adenyl nucleotide binding
binding
catalytic activity
disulfide oxidoreductase activity
FAD or FADH2 binding
glutathione disulfide oxidoreductase activity
glutathione-disulfide reductase activity
NADP or NADPH binding
nucleoside binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on a sulfur group of donors
peptide disulfide oxidoreductase activity
purine nucleoside binding
Process
cell redox homeostasis
cellular homeostasis
cellular metabolic process
cellular process
glutathione metabolic process
metabolic process
oxidation reduction
peptide metabolic process
Gene Properties
Blattner:b3500
Gene OrientationClockwise
Centisome Percentage:78.55
Left Sequence End3644322
Right Sequence End3645674
Gene Sequence:
>1353 bp
ATGCTGAGTTTTCTCTGGGATTTGGCTTCGTTCATCGTTGCACTGGGTGTACTTATCACC
GTGCATGAATTTGGTCATTTCTGGGTTGCCCGGCGTTGTGGTGTTCGCGTTGAGCGTTTC
TCAATAGGGTTTGGTAAGGCGCTCTGGCGGCGAACTGATAAGCTCGGCACCGAATATGTT
ATCGCCCTGATCCCGTTGGGCGGTTATGTCAAAATGCTGGATGAGCGCGCAGAACCGGTC
GTTCCGGAACTCCGCCACCATGCCTTCAATAATAAATCTGTCGGCCAACGAGCGGCGATT
ATTGCCGCAGGTCCGGTTGCAAACTTCATTTTTGCTATCTTTGCCTACTGGCTGGTTTTT
ATTATTGGTGTGCCTGGCGTACGTCCGGTGGTTGGCGAAATAGCAGCCAATTCGATAGCT
GCGGAAGCACAAATTGCACCAGGTACGGAACTAAAAGCCGTAGATGGTATCGAAACGCCT
GATTGGGATGCCGTGCGTTTGCAGTTGGTCGATAAAATTGGCGATGAAAGCACCACCATT
ACAGTAGCGCCATTTGGCAGCGACCAACGGCGGGATGTAAAGCTCGATTTACGTCACTGG
GCGTTTGAGCCTGATAAAGAAGATCCGGTATCTTCGCTGGGGATTCGTCCTCGTGGGCCG
CAAATTGAACCTGTACTGGAAAATGTGCAGCCAAACTCGGCGGCAAGCAAGGCAGGTTTG
CAAGCAGGCGACAGGATCGTTAAAGTCGATGGTCAGCCCTTAACGCAGTGGGTGACCTTT
GTGATGCTTGTCCGGGATAACCCGGGTAAATCCTTAGCGTTAGAAATCGAAAGGCAGGGG
AGTCCCTTGTCTTTGACATTAATCCCGGAGAGTAAACCGGGTAATGGTAAAGCGATTGGT
TTTGTCGGTATTGAGCCGAAAGTCATTCCTTTGCCAGATGAGTATAAAGTTGTACGCCAG
TATGGGCCGTTCAACGCCATCGTCGAAGCCACGGACAAAACGTGGCAGCTGATGAAGCTG
ACGGTCAGTATGCTGGGAAAATTGATCACCGGTGATGTGAAACTGAACAACCTCAGTGGG
CCGATCTCTATCGCCAAGGGGGCTGGGATGACAGCGGAACTCGGGGTTGTTTATTACCTG
CCGTTTCTTGCGCTTATTAGCGTGAACTTAGGGATAATTAACCTGTTTCCGTTGCCCGTA
CTTGACGGGGGGCATCTGCTGTTCCTTGCGATCGAAAAGATCAAGGGCGGACCGGTATCC
GAGCGGGTTCAAGACTTTTGTTATCGCATTGGCTCGATTCTGCTGGTGCTGTTAATGGGG
CTTGCACTTTTCAATGATTTCTCTCGGTTATGA
Protein Properties
Pfam Domain Function:
Protein Residues:450
Protein Molecular Weight:48772
Protein Theoretical pI:6
PDB File:1GET
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glutathione reductase
MTKHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIR
EAIHMYGPDYGFDTTINKFNWETLIASRTAYIDRIHTSYENVLGKNNVDVIKGFARFVDA
KTLEVNGETITADHILIATGGRPSHPDIPGVEYGIDSDGFFALPALPERVAVVGAGYIAV
ELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNTDG
SLTLELEDGRSETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYA
VGDNTGAVELTPVAVAAGRRLSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAR
EQYGDDQVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFGMDEMLQGFA
VALKMGATKKDFDNTVAIHPTAAEEFVTMR
References
External Links:
ResourceLink
Uniprot ID:P06715
Uniprot Name:GSHR_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902917
PDB ID:1GET
Ecogene ID:EG10412
Ecocyc:EG10412
ColiBase:b3500
Kegg Gene:b3500
EchoBASE ID:EB0407
CCDB:GSHR_ECOLI
BacMap:16131372
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
  • Ermler, U., Schulz, G. E. (1991). "The three-dimensional structure of glutathione reductase from Escherichia coli at 3.0 A resolution." Proteins 9:174-179. Pubmed: 2006135
  • Greer, S., Perham, R. N. (1986). "Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases." Biochemistry 25:2736-2742. Pubmed: 3521741
  • 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
  • Mittl, P. R., Schulz, G. E. (1994). "Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes." Protein Sci 3:799-809. Pubmed: 8061609
  • Sofia, H. J., Burland, V., Daniels, D. L., Plunkett, G. 3rd, Blattner, F. R. (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 22:2576-2586. Pubmed: 8041620