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.

UniProtKB Entries (1)

Q81X77
GPMI_BACAN
Bacillus anthracis
2,3-bisphosphoglycerate-independent phosphoglycerate mutase

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.
Nukui, M., Mello, L.V., Littlejohn, J.E., Setlow, B., Setlow, P., Kim, K., Leighton, T., Jedrzejas, M.J.
Biophys.J.