CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.870 | DHBP synthase |
|
3.90.870.10 | DHBP synthase |
Domain Context
CATH Clusters
| Superfamily | DHBP synthase |
| Functional Family | Riboflavin biosynthesis protein RibBA |
Enzyme Information
| 3.5.4.25 |
GTP cyclohydrolase II.
based on mapping to UniProt A5U2B7
GTP + 3 H(2)O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D- ribosylamino)pyrimidine + diphosphate.
-!- Two C-N bonds are hydrolyzed, releasing formate, with simultaneous removal of the terminal diphosphate.
|
| 4.1.99.12 |
3,4-dihydroxy-2-butanone-4-phosphate synthase.
based on mapping to UniProt A5U2B7
D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate.
-!- The reaction involves an intramolecular skeletal rearrangement, with the bonds in D-ribulose 5-phosphate that connect C-3 and C-5 to C-4 being broken, C-4 being removed as formate and reconnection of C-3 and C-5. -!- The phosphorylated four-carbon product (L-3,4-dihydroxybutan-2-one 4-phosphate) is an intermediate in the biosynthesis of riboflavin.
|
UniProtKB Entries (1)
| A5U2B7 |
RIBBA_MYCTA
Mycobacterium tuberculosis H37Ra
Riboflavin biosynthesis protein RibBA
|
PDB Structure
| PDB | 4I14 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The crystal structure reveals the molecular mechanism of bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II (Rv1415) from Mycobacterium tuberculosis
Acta Crystallogr.,Sect.D
|
