Glutathione reductase

Details

Name
Glutathione reductase
Synonyms
  • 1.8.1.7
  • GR
Gene Name
gor
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016057|Glutathione reductase
MTKHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIR
EAIHMYGPDYGFDTTINKFNWETLIASRTAYIDRIHTSYENVLGKNNVDVIKGFARFVDA
KTLEVNGETITADHILIATGGRPSHPDIPGVEYGIDSDGFFALPALPERVAVVGAGYIAV
ELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNTDG
SLTLELEDGRSETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYA
VGDNTGAVELTPVAVAAGRRLSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAR
EQYGDDQVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFGMDEMLQGFA
VALKMGATKKDFDNTVAIHPTAAEEFVTMR
Number of residues
450
Molecular Weight
48772.195
Theoretical pI
5.88
GO Classification
Functions
FAD binding / glutathione-disulfide reductase activity / NADP binding
Processes
cell redox homeostasis / glutathione metabolic process
Components
cytoplasm / membrane
General Function
Nadp binding
Specific Function
Maintains high levels of reduced glutathione in the cytosol.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0016058|Glutathione reductase (gor)
ATGACTAAACACTATGATTACATCGCCATCGGCGGCGGCAGCGGCGGTATCGCCTCCATC
AACCGCGCGGCTATGTACGGCCAGAAATGTGCGCTGATTGAAGCCAAAGAGCTGGGCGGC
ACCTGCGTAAATGTTGGCTGTGTGCCGAAAAAAGTGATGTGGCACGCGGCGCAAATCCGT
GAAGCGATCCATATGTACGGCCCGGATTATGGTTTTGATACCACTATCAATAAATTCAAC
TGGGAAACGTTGATCGCCAGCCGTACCGCCTATATCGACCGTATTCATACTTCCTATGAA
AACGTGCTCGGTAAAAATAACGTTGATGTAATCAAAGGCTTTGCCCGCTTCGTTGATGCC
AAAACGCTGGAGGTAAACGGCGAAACCATCACGGCCGATCATATTCTGATCGCCACAGGC
GGTCGTCCGAGCCACCCGGATATTCCGGGCGTGGAATACGGTATTGATTCTGATGGCTTC
TTCGCCCTTCCTGCTTTGCCAGAGCGCGTGGCGGTTGTTGGCGCGGGTTACATCGCCGTT
GAGCTGGCGGGCGTGATTAACGGCCTCGGCGCGAAAACGCATCTGTTTGTGCGTAAACAT
GCGCCGCTGCGCAGCTTCGACCCGATGATTTCCGAAACGCTGGTCGAAGTGATGAACGCC
GAAGGCCCGCAGCTGCACACCAACGCCATCCCGAAAGCGGTAGTGAAAAATACCGATGGT
AGCCTGACGCTGGAGCTGGAAGATGGTCGCAGTGAAACGGTGGATTGCCTGATTTGGGCG
ATTGGTCGCGAGCCTGCCAATGACAACATCAACCTGGAAGCCGCTGGCGTTAAAACTAAC
GAAAAAGGCTATATCGTCGTCGATAAATATCAAAACACCAATATTGAAGGTATTTACGCG
GTGGGCGATAACACGGGTGCAGTGGAGCTGACACCGGTGGCAGTTGCAGCGGGTCGCCGT
CTCTCTGAACGCCTGTTTAATAACAAGCCGGATGAGCATCTGGATTACAGCAACATTCCG
ACCGTGGTCTTCAGCCATCCGCCGATTGGTACTGTTGGTTTAACGGAACCGCAGGCGCGC
GAGCAGTATGGCGACGATCAGGTGAAAGTGTATAAATCCTCTTTCACCGCGATGTATACC
GCCGTCACCACTCACCGCCAGCCGTGCCGCATGAAGCTGGTGTGCGTTGGATCGGAAGAG
AAGATTGTCGGTATTCACGGCATTGGCTTTGGTATGGACGAAATGTTGCAGGGCTTCGCG
GTGGCGCTGAAGATGGGGGCAACCAAAAAAGACTTCGACAATACCGTCGCCATTCACCCA
ACGGCGGCAGAAGAGTTCGTGACAATGCGTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP06715
UniProtKB Entry NameGSHR_ECOLI
GenBank Protein ID146248
GenBank Gene IDM13141
General References
  1. Greer S, Perham RN: Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases. Biochemistry. 1986 May 6;25(9):2736-42. [Article]
  2. Sofia HJ, Burland V, Daniels DL, Plunkett G 3rd, Blattner FR: Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes. Nucleic Acids Res. 1994 Jul 11;22(13):2576-86. [Article]
  3. 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]
  4. 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]
  5. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  6. Ermler U, Schulz GE: The three-dimensional structure of glutathione reductase from Escherichia coli at 3.0 A resolution. Proteins. 1991;9(3):174-9. [Article]
  7. Mittl PR, Schulz GE: Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes. Protein Sci. 1994 May;3(5):799-809. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00336Nitrofuralapproved, investigational, vet_approvedyesinhibitorDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails