An FMN hydrolase is fused to a riboflavin kinase homolog in plants.

@article{Sandoval2005AnFH,
  title={An FMN hydrolase is fused to a riboflavin kinase homolog in plants.},
  author={Francisco J. Sandoval and Sanja Roje},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 46},
  pages={38337-45}
}
Riboflavin kinases catalyze synthesis of FMN from riboflavin and ATP. These enzymes have to date been cloned from bacteria, yeast, and mammals, but not from plants. Bioinformatic approaches suggested that diverse plant species, including many angiosperms, two gymnosperms, a moss (Physcomitrella patens), and a unicellular green alga (Chlamydomonas reinhardtii), encode proteins that are homologous to riboflavin kinases of yeast and mammals, but contain an N-terminal domain that belongs to the… CONTINUE READING