| FAD synthetase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of flavin binding to fad synthetase from thermotoga maritina | |||||||||
| Identifiers | |||||||||
| Symbol | FAD_syn | ||||||||
| Pfam | PF06574 | ||||||||
| Pfam clan | CL0119 | ||||||||
| InterPro | IPR015864 | ||||||||
| SCOP2 | 1n05 / SCOPe / SUPFAM | ||||||||
| |||||||||
The prokaryotic riboflavin biosynthesis protein is a bifunctional enzyme found in bacteria that catalyzes the phosphorylation of riboflavin into flavin mononucleotide (FMN) and the adenylylation of FMN into flavin adenine dinucleotide (FAD). It consists of a C-terminal riboflavin kinase and an N-terminal FMN-adenylyltransferase. This bacterial protein is functionally similar to the monofunctional riboflavin kinases and FMN-adenylyltransferases of eukaryotic organisms, but only the riboflavin kinases are structurally homologous.