Literature summary for 1.17.5.3 extracted from

Simon, J.; van Spanning, R.J.; Richardson, D.J.
The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems (2008), Biochim. Biophys. Acta, 1777, 1480-1490.

Search for more literature for 1.17.5.3

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	in the proton motive system of the formate dehydrogenase the donor oxidation and quinone reduction sites are located at opposite sides of the membrane	Escherichia coli	16020	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
formate + a quinone	Escherichia coli	in the proton motive system of the formate dehydrogenase the donor oxidation and quinone reduction sites are located at opposite sides of the membrane. The formate dehydrogenase (Fdh-N or FdnGHI complex) and nitrate reductase A (NarA or NarGHI complex) together form the paradigmatic Fdh-Nar full redox loop	CO2 + a quinol	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
formate + a quinone	in the proton motive system of the formate dehydrogenase the donor oxidation and quinone reduction sites are located at opposite sides of the membrane. The formate dehydrogenase (Fdh-N or FdnGHI complex) and nitrate reductase A (NarA or NarGHI complex) together form the paradigmatic Fdh-Nar full redox loop	Escherichia coli	CO2 + a quinol	-	?

Synonyms

Synonyms	Comment	Organism
Fdh-N	-	Escherichia coli
fdnGHI	-	Escherichia coli

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Release 2023.1 (January 2023)