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

• Pyr_redox_2 (PF07992)
• Pyr_redox_dim (PF02852)

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

Resource	Link
UniProtKB ID	P06715
UniProtKB Entry Name	GSHR_ECOLI
GenBank Protein ID	146248
GenBank Gene ID	M13141

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 ID	Name	Drug group	Pharmacological action?	Actions	Details
DB00336	Nitrofural	approved, investigational, vet_approved, withdrawn	yes	inhibitor	Details
DB03147	Flavin adenine dinucleotide	approved	unknown		Details