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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)
FAD synthetase family protein
FAD synthetase family protein containing only the N-terminal domain of a bifunctional enzyme such as Rhodococcus opacus putative bifunctional riboflavin kinase/FMN adenylyltransferase; may catalyze the the adenylation of FMN to FAD, but not the phosphorylation of riboflavin
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