| Accession |
MF_00180 |
| Dates |
1-JUN-2001 (Created) 7-JUN-2008 (Last updated, Version 15) |
| Protein name |
| RecName: |
Full=3,4-dihydroxy-2-butanone 4-phosphate synthase; Short=DHBP synthase; EC=4.1.99.12; |
|
FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate (By similarity).
CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate.
COFACTOR: Binds 2 divalent metal cations per subunit. Magnesium or manganese (By similarity).
PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 3,4-dihydroxy-2-butanone 4-phosphate from D-ribulose 5-phosphate: step 1/1.
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the DHBP synthase family.
GO:0000287; Molecular function: magnesium ion binding.
GO:0008686; Molecular function: 3,4-dihydroxy-2-butanone-4-phosphate synthase activity.
GO:0030145; Molecular function: manganese ion binding.
GO:0009231; Biological process: riboflavin biosynthetic process.
| From: RIBB_METJA (Q60364) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| REGION |
|
25 |
|
26 |
|
Substrate binding (By similarity) |
|
R-E |
|
|
| REGION |
|
161 |
|
165 |
|
Substrate binding (By similarity) |
|
R-x-x-[HQ]-T |
|
|
| METAL |
|
26 |
|
26 |
|
Magnesium or manganese 1 (By similarity) |
|
E |
|
|
| METAL |
|
26 |
|
26 |
|
Magnesium or manganese 2 (By similarity) |
|
E |
|
|
| METAL |
|
164 |
|
164 |
|
Magnesium or manganese 2 (By similarity) |
|
H |
|
|
| BINDING |
|
30 |
|
30 |
|
Substrate (By similarity) |
|
D |
|
|
| BINDING |
|
185 |
|
185 |
|
Substrate (By similarity) |
|
E |
|
|
| SITE |
|
147 |
|
147 |
|
Essential for catalytic activity (By similarity) |
|
H |
|
|
| SITE |
|
185 |
|
185 |
|
Essential for catalytic activity (By similarity) |
|
E |
|
|
| Size range: |
200-247 amino acids |
| Related UniRules: |
MF_01283 (RIBBA (supersedes the current rule)) |
| Template: |
P0A7J0 (RIBB_ECOLI); Q60364 (RIBB_METJA): [Recover all] |
| Scope: |
Bacteria
Archaea |
| Fusion: |
Nter: None; Cter: <ribA-like> |
| Duplicate: |
None |
| Plasmid encoded: |
in RALSO |
| Comments: |
RibA and RibB are fused in some organisms (see MF_01283 for bifunctional RibBA). Some ribB are followed by a ribA-like domain, which does not seem to code for GTP cyclohydrolase II activity because it lacks all the residues important for activity. |
View rule in raw text format (no links)