Literature summary for 1.3.7.11 extracted from

Xu, Q.; Eguchi, T.; Mathews, I.I.; Rife, C.L.; Chiu, H.J.; Farr, C.L.; Feuerhelm, J.; Jaroszewski, L.; Klock, H.E.; Knuth, M.W.; Miller, M.D.; Weekes, D.; Elsliger, M.A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
Insights into substrate specificity of geranylgeranyl reductases revealed by the structure of digeranylgeranylglycerophospholipid reductase, an essential enzyme in the biosynthesis of archaeal membrane lipids (2010), J. Mol. Biol., 404, 403-417.

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with flavin adenine dinucleotide, to 1.6 A resolution. Substrate binding likely involves conformational changes, which are coupled to the two conformational states of the FAD cofactor	Thermoplasma acidophilum

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
43400	-	x * 43400, calculated	Thermoplasma acidophilum

Organism	UniProt	Comment	Textmining
Thermoplasma acidophilum	Q9HKS9	-	-

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2,3-di-O-geranylgeranylglyceryl phosphate + 16 reduced ferredoxin [iron-sulfur] cluster + 16 H+	-	Thermoplasma acidophilum	2,3-di-O-phytanylglyceryl phosphate + 16 oxidized ferredoxin [iron-sulfur] cluster	-	?

Subunits	Comment	Organism
?	x * 43400, calculated	Thermoplasma acidophilum

Synonyms	Comment	Organism
Ta0516	-	Thermoplasma acidophilum

Cofactor	Comment	Organism	Structure
FAD	-	Thermoplasma acidophilum

Organism	Comment	pI Value Maximum	pI Value
Thermoplasma acidophilum	calculated	-	7

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Release 2023.1 (January 2023)