CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
6 | Special |
|
6.10 | Helix non-globular |
|
6.10.250 | Single alpha-helices involved in coiled-coils or other helix-helix interfaces |
|
6.10.250.1180 |
Domain Context
CATH Clusters
| Superfamily | 6.10.250.1180 |
| Functional Family |
Enzyme Information
| 4.1.2.13 |
Fructose-bisphosphate aldolase.
based on mapping to UniProt B1YAL1
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
-!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7.
|
| 3.1.3.11 |
Fructose-bisphosphatase.
based on mapping to UniProt B1YAL1
D-fructose 1,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate.
-!- The animal enzyme also acts on sedoheptulose 1,7-bisphosphate.
|
UniProtKB Entries (1)
| B1YAL1 |
FBPAP_PYRNV
Pyrobaculum neutrophilum V24Sta
Fructose-1,6-bisphosphate aldolase/phosphatase
|
PDB Structure
| PDB | 3T2E |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase.
Nature
|
