CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.300 | P-loop containing nucleotide triphosphate hydrolases |
Domain Context
CATH Clusters
| Superfamily | P-loop containing nucleotide triphosphate hydrolases |
| Functional Family | 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 3 isoform 2 |
Enzyme Information
| 2.7.1.105 |
6-phosphofructo-2-kinase.
based on mapping to UniProt P25114
ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.
-!- Not identical with EC 2.7.1.11. -!- The enzyme copurifies with EC 3.1.3.46.
|
| 3.1.3.46 |
Fructose-2,6-bisphosphate 2-phosphatase.
based on mapping to UniProt P25114
Beta-D-fructose 2,6-bisphosphate + H(2)O = D-fructose 6-phosphate + phosphate.
-!- The enzyme copurifies with EC 2.7.1.105 (cf. EC 3.1.3.54).
|
UniProtKB Entries (1)
| P25114 |
F264_RAT
Rattus norvegicus
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4
|
PDB Structure
| PDB | 2BIF |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of the H256A mutant of rat testis fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase. Fructose 6-phosphate in the active site leads to mechanisms for both mutant and wild type bisphosphatase activities.
J.Biol.Chem.
|
