CATH Classification
Domain Context
CATH Clusters
| Superfamily | BPG-independent phosphoglycerate mutase, domain B |
| 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 Q81X77
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.
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UniProtKB Entries (1)
| Q81X77 |
GPMI_BACAN
Bacillus anthracis
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
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PDB Structure
| PDB | 2IFY |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure and Molecular Mechanism of Bacillus anthracis Cofactor-Independent Phosphoglycerate Mutase: A Crucial Enzyme for Spores and Growing Cells of Bacillus Species.
Biophys.J.
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