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 | 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.
Sci Rep
|
