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Literature summary extracted from

  • Alves, E.; Henriques, B.J.; Rodrigues, J.V.; Prudencio, P.; Rocha, H.; Vilarinho, L.; Martinho, R.G.; Gomes, C.M.
    Mutations at the flavin binding site of ETF:QO yield a MADD-like severe phenotype in Drosophila (2012), Biochim. Biophys. Acta, 1822, 1284-1292.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.5.1 gene CG12140, mapping and cloning of ETF:QO alleles, expression of the two subunits ETFA and ETFB in Escherichia coli strain BL21 Drosophila melanogaster

Protein Variants

EC Number Protein Variants Comment Organism
1.5.5.1 additional information three independent mutant alleles, corresponding to three distinct point mutations in ETF:QO, are lethal as a result of a specific knockdown of FAD binding by direct disruption of the cofactor binding motif within the nucleotide binding Rossmann fold, a nucleotide binding structural domain also present in ETF:QO, which comprises a beta-strand connected by a short loop to an alpha-helix, and includes an expanded sequence motif (V/IxGx1–2GxxGxxxG/A) that affords both FAD binding and stabilisation of the secondary structure elements involved, overview Drosophila melanogaster

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.5.1 reduced electron-transferring flavoprotein + ubiquinone Drosophila melanogaster
-
electron-transferring flavoprotein + ubiquinol
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.5.5.1 Drosophila melanogaster
-
gene CG12140
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.5.1 additional information assay method uses dichlorophenolindophenol, DCPIP, as substrate Drosophila melanogaster ?
-
?
1.5.5.1 reduced electron-transferring flavoprotein + ubiquinone
-
Drosophila melanogaster electron-transferring flavoprotein + ubiquinol
-
?

Synonyms

EC Number Synonyms Comment Organism
1.5.5.1 electron transfer flavoprotein:ubiquinone oxidoreductase
-
Drosophila melanogaster
1.5.5.1 ETF:QO
-
Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.5.1 7.5
-
assay at Drosophila melanogaster

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.5.1 FAD
-
Drosophila melanogaster

General Information

EC Number General Information Comment Organism
1.5.5.1 malfunction ETF:QO mutant alleles faileto identify developmental defects, but a complete dysfunction of the ETF:QO protein leads to abnormal mitochondrial fatty acid oxidation. Acylcarnitine levels in ETF:QO mutant embryos display a profile typical of MADD, i.e. multiple acyl-CoA dehydrogenase deficiency, a metabolic disease of bet-oxidation, with a broad range of clinical phenotypes, varying from embryonic lethal to mild forms in humans. Fly mutant phentypes, overview Drosophila melanogaster
1.5.5.1 additional information the Rossmann fold is a nucleotide binding structural domain present in ETF:QO, it comprises a beta-strand connected by a short loop to an alpha-helix, and includes an expanded sequence motif (V/IxGx1-2GxxGxxxG/A) that affords both FAD binding and stabilisation of the secondary structure elements involved Drosophila melanogaster
1.5.5.1 physiological function the enzyme is maternally required for Drosophila embryogenesis Drosophila melanogaster