Literature summary extracted from

Nishizawa, A.; Harada, A.; Senda, M.; Tachihara, Y.; Muramatsu, D.; Kishigami, S.; Mori, S.; Sugiyama, K.; Senda, T.; Kimura, S.
Complete pyridine-nucleotide-specific conversion of an NADH-dependent ferredoxin reductase (2014), Biochem. J., 462, 257-265 .

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.18.1.3	expressed in Escherichia coli JM109 cells	Acidovorax sp. KKS102

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1.18.1.3	reduced [2Fe-2S] ferredoxin + NAD+ + H+	Acidovorax sp. KKS102	-	oxidized [2Fe-2S] ferredoxin + NADH	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.18.1.3	Acidovorax sp. KKS102	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.18.1.3	Blue-sepharose column chromatography	Acidovorax sp. KKS102

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.18.1.3	ferricyanide + NADH	-	Acidovorax sp. KKS102	ferrocyanide + NAD+ + H+	-	?
1.18.1.3	reduced [2Fe-2S] ferredoxin + NAD+ + H+	-	Acidovorax sp. KKS102	oxidized [2Fe-2S] ferredoxin + NADH	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
1.18.1.3	BphA4	an NADH-specific ferredoxin reductase component of biphenyl dioxygenase BphA	Acidovorax sp. KKS102
1.18.1.3	FdR	-	Acidovorax sp. KKS102
1.18.1.3	NADH-dependent ferredoxin reductase	-	Acidovorax sp. KKS102

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.18.1.3	NAD+	-	Acidovorax sp. KKS102

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Release 2023.1 (January 2023)