CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.620 | HUPs |
Domain Context
CATH Clusters
| Superfamily | HUPs |
| Functional Family | Riboflavin biosynthesis protein RibF |
Enzyme Information
| 2.7.1.26 |
Riboflavin kinase.
based on mapping to UniProt A0A0H2UPY5
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 A0A0H2UPY5
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)
| A0A0H2UPY5 |
A0A0H2UPY5_STRPN
Streptococcus pneumoniae TIGR4
Riboflavin biosynthesis protein
|
PDB Structure
| PDB | 3OP1 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal Structure of Macrolide-efflux Protein SP_1110 from Streptococcus pneumoniae
TO BE PUBLISHED
|
