CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.720 | Alkaline Phosphatase, subunit A |
|
3.40.720.10 | Alkaline Phosphatase, subunit A |
Domain Context
CATH Clusters
| Superfamily | Alkaline Phosphatase, subunit A |
| Functional Family | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase |
Enzyme Information
| 5.4.2.12 |
Phosphoglycerate mutase (2,3-diphosphoglycerate-independent).
based on mapping to UniProt Q2G029
2-phospho-D-glycerate = 3-phospho-D-glycerate.
-!- The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. -!- Cf. EC 5.4.2.11. -!- The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. -!- Both metal ions are involved in the reaction. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1.
|
UniProtKB Entries (1)
| Q2G029 |
Q2G029_STAA8
Staphylococcus aureus subsp. aureus NCTC 8325
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
|
PDB Structure
| PDB | 4NWJ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Complete catalytic cycle of cofactor-independent phosphoglycerate mutase involves a spring-loaded mechanism
Febs J.
|
