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FAD synthetase
This family corresponds to the N terminal domain of the bifunctional enzyme riboflavin kinase / FAD synthetase. These enzymes have both ATP:riboflavin 5'-phospho transferase and ATP:FMN-adenylyltransferase activity [1]. They catalyse the 5'-phosphorylation of riboflavin to FMN and the adenylylation of FMN to FAD [1]. This domain is thought to have the flavin mononucleotide (FMN) adenylyltransferase activity [2]. [1]. 3023344. Purification and characterization of FAD synthetase from. Brevibacterium ammoniagenes.. Manstein DJ, Pai EF;. J Biol Chem 1986;261:16169-16173.. [2]. 15468322. Crystal structure of flavin binding to FAD synthetase of. Thermotoga maritima.. Wang W, Kim R, Yokota H, Kim SH;. Proteins 2005;58:246-248. (from Pfam)
riboflavin kinase
This family represents the C-terminal region of the bifunctional riboflavin biosynthesis protein known as RibC in Bacillus subtilis. The RibC protein from Bacillus subtilis has both flavokinase and flavin adenine dinucleotide synthetase (FAD-synthetase) activities. RibC plays an essential role in the flavin metabolism [1]. This domain is thought to have kinase activity [2]. [1]. 9473052. Regulation of riboflavin biosynthesis in Bacillus subtilis is. affected by the activity of the flavokinase/flavin adenine. dinucleotide synthetase encoded by ribC.. Mack M, van Loon AP, Hohmann HP;. J Bacteriol 1998;180:950-955.. [2]. 15468322. Crystal structure of flavin binding to FAD synthetase of. Thermotoga maritima.. Wang W, Kim R, Yokota H, Kim SH;. Proteins 2005;58:246-248. (from Pfam)
bifunctional riboflavin kinase/FMN adenylyltransferase
bifunctional riboflavin biosynthesis protein having both ATP-riboflavin kinase and ATP-flavin mononucleotide adenylyltransferase activities
riboflavin biosynthesis protein RibF
multifunctional enzyme: riboflavin kinase (EC 2.7.1.26) (flavokinase) / FMN adenylyltransferase (EC 2.7.7.2) (FAD pyrophosphorylase) (FAD synthetase).
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