| Accession |
MF_01283 |
| Dates |
16-NOV-2007 (Created) 27-SEP-2010 (Last updated, Version 7) |
| Protein name |
| RecName: |
Full=Riboflavin biosynthesis protein ribBA; |
| RecName: |
Full=3,4-dihydroxy-2-butanone 4-phosphate synthase; Short=DHBP synthase; EC=4.1.99.12; |
| RecName: |
Full=GTP cyclohydrolase-2; EC=3.5.4.25; |
| AltName: |
Full=GTP cyclohydrolase II; |
|
FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate (By similarity).
FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate (By similarity).
CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate.
CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.
COFACTOR: Binds 2 divalent metal cations per subunit. Magnesium or manganese (By similarity).
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.
SIMILARITY: In the N-terminal section; belongs to the DHBP synthase family.
SIMILARITY: In the C-terminal section; belongs to the GTP cyclohydrolase II family.
GO:0000287; Molecular function: magnesium ion binding.
GO:0003935; Molecular function: GTP cyclohydrolase II activity.
GO:0008270; Molecular function: zinc 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: RIBBA_BACSU (P17620) |
| Key |
|
From |
|
To |
|
Description |
|
Condition |
|
FTGroup |
| NP_BIND |
|
251 |
|
255 |
|
GTP (By similarity) |
|
|
|
|
| NP_BIND |
|
294 |
|
296 |
|
GTP (By similarity) |
|
E-G-R |
|
|
| REGION |
|
Nter |
|
199 |
|
DHBP synthase |
|
|
|
|
| REGION |
|
26 |
|
27 |
|
D-ribulose 5-phosphate binding (By similarity) |
|
R-E |
|
|
| REGION |
|
138 |
|
142 |
|
D-ribulose 5-phosphate binding (By similarity) |
|
R-x-x-H-T |
|
|
| REGION |
|
200 |
|
Cter |
|
GTP cyclohydrolase II |
|
|
|
|
| ACT_SITE |
|
328 |
|
328 |
|
Proton acceptor; for GTP cyclohydrolase activity (Potential) |
|
D |
|
|
| ACT_SITE |
|
330 |
|
330 |
|
Nucleophile; for GTP cyclohydrolase activity (By similarity) |
|
R |
|
|
| METAL |
|
27 |
|
27 |
|
Magnesium or manganese 1 (By similarity) |
|
E |
|
|
| METAL |
|
27 |
|
27 |
|
Magnesium or manganese 2 (By similarity) |
|
E |
|
|
| METAL |
|
141 |
|
141 |
|
Magnesium or manganese 2 (By similarity) |
|
H |
|
|
| METAL |
|
256 |
|
256 |
|
Zinc; catalytic (By similarity) |
|
C |
|
|
| METAL |
|
267 |
|
267 |
|
Zinc; catalytic (By similarity) |
|
C |
|
|
| METAL |
|
269 |
|
269 |
|
Zinc; catalytic (By similarity) |
|
C |
|
|
| BINDING |
|
31 |
|
31 |
|
D-ribulose 5-phosphate (By similarity) |
|
D |
|
|
| BINDING |
|
162 |
|
162 |
|
D-ribulose 5-phosphate (By similarity) |
|
E |
|
|
| BINDING |
|
272 |
|
272 |
|
GTP (By similarity) |
|
Q |
|
|
| BINDING |
|
316 |
|
316 |
|
GTP (By similarity) |
|
T |
|
|
| BINDING |
|
351 |
|
351 |
|
GTP (By similarity) |
|
[TS] |
|
|
| BINDING |
|
356 |
|
356 |
|
GTP (By similarity) |
|
K |
|
|
| SITE |
|
124 |
|
124 |
|
Essential for DHBP synthase activity (By similarity) |
|
H |
|
|
| SITE |
|
162 |
|
162 |
|
Essential for DHBP synthase activity (By similarity) |
|
E |
|
|
| Size range: |
388-425 amino acids |
| Related UniRules: |
MF_00178 (RISB); MF_00179 (RIBA) |
| Template: |
P50855 (RIBBA_ACTPL) |
| Scope: |
Bacteria |
| Fusion: |
Nter: None; Cter: <Unknown> |
| Duplicate: |
None |
| Plasmid encoded: |
None |
| Comments: |
RibA and RibB are not fused in some organisms (see MF_00179 for RibA and MF_00180 for RibB). Fused with an unknown C-terminal domain in SYNY3. |
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