CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.120 | Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3 |
|
3.40.120.10 | Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3 |
Domain Context
CATH Clusters
| Superfamily | Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3 |
| Functional Family | Phosphoglucomutase 5 |
Enzyme Information
| 5.4.2.2 |
Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
based on mapping to UniProt P47244
Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
-!- Maximum activity is only obtained in the presence of alpha-D-glucose 1,6-bisphosphate. -!- This bisphosphate is an intermediate in the reaction, being formed by transfer of a phosphate residue from the enzyme to the substrate, but the dissociation of bisphosphate from the enzyme complex is much slower than the overall isomerization. -!- Also, more slowly, catalyzes the interconversion of 1-phosphate and 6-phosphate isomers of many other alpha-D-hexoses, and the interconversion of alpha-D-ribose 1-phosphate and 5-phosphate. -!- Cf. EC 5.4.2.5. -!- Formerly EC 2.7.5.1.
|
UniProtKB Entries (1)
| P47244 |
PGM1_PARTE
Paramecium tetraurelia
Phosphoglucomutase-1
|
PDB Structure
| PDB | 1KFI |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure analysis of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase), from Paramecium reveals significant conformational variability.
J.Mol.Biol.
|
