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Literature summary for 1.5.5.1 extracted from

  • Li, Y.; Zhu, J.; Hu, J.; Meng, X.; Zhang, Q.; Zhu, K.; Chen, X.; Chen, X.; Li, G.; Wang, Z.; Lu, G.
    Functional characterization of electron-transferring flavoprotein and its dehydrogenase required for fungal development and plant infection by the rice blast fungus (2016), Sci. Rep., 6, 24911 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
cloning of the electron-transferring flavoprotein (ETF) alpha and beta subunit encoding genes ETFA and ETFB and enzyme ETFDH encoding gene ETFDH from Magnaporthe oryzae, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of GFP-tagged genes ETFA, ETFB, and ETFDH in Magnaporthe oryzae cells Pyricularia oryzae

Protein Variants

Protein Variants Comment Organism
additional information generation of gene deletion mutants of the two ETF genes (ETFA and ETFB) and the ETFDH gene (ETFDH) by targeted gene deletion mutagenesis, mutant are named etfa?, etfb? and etfdh? respectively. ETF and ETFDH mutants display growth and conidiation defects, phenotypes, overview Pyricularia oryzae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion Magnaporthe oryzae ETF and ETFDH co-localization with the mitochondrial marker ATP1-RFP, but almost not with the peroxysomal marker PTS1-RFP Pyricularia oryzae 5739
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Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ enzyme ETFDH is a monomer containing a FAD molecule and an iron-sulfur cluster Pyricularia oryzae

Organism

Organism UniProt Comment Textmining
Pyricularia oryzae G4MVI8
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
reduced electron-transferring flavoprotein + ubiquinone electron-transferring flavoprotein alpha- and beta-subunits contain a FAD cofactor and an AMP molecule, respectively Pyricularia oryzae electron-transferring flavoprotein + ubiquinol
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?

Subunits

Subunits Comment Organism
More proteins ETFB and ETFDH contain an ETF domain and an ETFDH domain, respectively, while protein ETFA also contains a FAD binding domain in addition to the ETF domain Pyricularia oryzae

Synonyms

Synonyms Comment Organism
ETF dehydrogenase
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Pyricularia oryzae

Cofactor

Cofactor Comment Organism Structure
FAD enzyme ETFDH is a monomer containing a FAD molecule and an iron-sulfur cluster Pyricularia oryzae
iron-sulfur center enzyme ETFDH is a monomer containing a FAD molecule and an iron-sulfur cluster Pyricularia oryzae
ubiquinone
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Pyricularia oryzae

General Information

General Information Comment Organism
malfunction a small number of conidia are formed by ETF and ETFDH deletion mutants growing on different media, the conidial germination and appressoria formation on hydrophobic surface do not show any variations compared to the wild-type. Sprayed onto live barley and rice seedlings, the mutant conidia are almost completely non-pathogenic, despite producing a few non-extended necroses on the host surface. ETF and ETFDH mutants display growth and conidiation defects. ETF mutant etfb- cells exhibit reduced turgor pressure in 2-4 M glycerol, reduced ATP synthesis, and the ETF mutant etfb- is more sensitive to host oxidative stress (by H2O2 in host cells). ETF mutant etfb- shows lipid body accumulation. Phenotypes, overview Pyricularia oryzae
physiological function electron-transferring flavoprotein (ETF) and its dehydrogenase (ETFDH) are highly conserved electron carriers which mainly function in mitochondrial fatty acid beta oxidation. Besides catalyzing dehydrogenation, acyl-CoA dehydrogenases also transfer electrons to an electron-transferring flavoprotein (ETF), which, through the electron-transferring flavoprotein dehydrogenase (ETFDH), finally delivers the electrons to the ubiquinone pool in the terminal respiratory system for ATP synthesis. Thus, ETF and ETFDH link the fatty acids oxidation with respiratory system Pyricularia oryzae