CATH Domain 3zugA02

CATH Classification

Level	CATH Code	Description
	2	Mainly Beta
	2.40	Beta Barrel
	2.40.30	Elongation Factor Tu (Ef-tu); domain 3
	2.40.30.30	Riboflavin kinase-like

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	3ZUG
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Key Residues at the Riboflavin Kinase Catalytic Site of the Bifunctional Riboflavin Kinase/Fmn Adenylyltransferase from Corynebacterium Ammoniagenes. Serrano, A., Frago, S., Herguedas, B., Martinez-Julvez, M., Velazquez-Campoy, A., Medina, M. Cell Biochem.Biophys.