CATH Classification

Domain Context

CATH Clusters

Superfamily Riboflavin kinase-like
Functional Family Riboflavin biosynthesis protein

Enzyme Information

2.7.1.26
Riboflavin kinase.
based on mapping to UniProt Q59263
ATP + riboflavin = ADP + FMN.
-!- The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B(6), vitamin B12 and folates. -!- While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2. -!- In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP.
2.7.7.2
FAD synthetase.
based on mapping to UniProt Q59263
ATP + FMN = diphosphate + FAD.
-!- Highly specific for ATP as phosphate donor. -!- The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates. -!- While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26.

UniProtKB Entries (1)

Q59263
RIBF_CORAM
Corynebacterium ammoniagenes
Bifunctional riboflavin kinase/FMN adenylyltransferase

PDB Structure

PDB 5FNZ
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes.
Serrano, A., Sebastian, M., Arilla-Luna, S., Baquedano, S., Herguedas, B., Velazquez-Campoy, A., Martinez-Julvez, M., Medina, M.
Sci Rep