CATH Classification

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 Q9X519
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)

Q9X519
GPMI_GEOSE
Geobacillus stearothermophilus
2,3-bisphosphoglycerate-independent phosphoglycerate mutase

PDB Structure

PDB 1EQJ
External Links
Method X-RAY DIFFRACTION
Organism Bacillus
Primary Citation
Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate.
Jedrzejas, M.J., Chander, M., Setlow, P., Krishnasamy, G.
J.Biol.Chem.