CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.310 | TATA-Binding Protein |
|
3.30.310.50 | Alpha-D-phosphohexomutase, C-terminal domain |
Domain Context
CATH Clusters
| Superfamily | Alpha-D-phosphohexomutase, C-terminal domain |
| Functional Family | Phosphomannomutase/phosphoglucomutase |
Enzyme Information
| 5.4.2.8 |
Phosphomannomutase.
based on mapping to UniProt P26276
Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
-!- Alpha-D-mannose 1,6-bisphosphate or alpha-D-glucose 1,6-bisphosphate can act as cofactor. -!- Formerly EC 2.7.5.7.
|
| 5.4.2.2 |
Phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent).
based on mapping to UniProt P26276
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)
| P26276 |
ALGC_PSEAE
Pseudomonas aeruginosa PAO1
Phosphomannomutase/phosphoglucomutase
|
PDB Structure
| PDB | 2H4L |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor.
Acta Crystallogr.,Sect.F
|
