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 kinase, putative |
Enzyme Information
| 2.7.1.26 |
Riboflavin kinase.
based on mapping to UniProt Q969G6
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.
|
UniProtKB Entries (1)
| Q969G6 |
RIFK_HUMAN
Homo sapiens
Riboflavin kinase
|
PDB Structure
| PDB | 1Q9S |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism.
Biochemistry
|
