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
- FunctionsFAD binding / glutathione-disulfide reductase activity / NADP bindingProcessescell redox homeostasis / glutathione metabolic processComponentscytoplasm / 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
Resource Link UniProtKB ID P06715 UniProtKB Entry Name GSHR_ECOLI GenBank Protein ID 146248 GenBank Gene ID M13141 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]