CATH Classification

Domain Context

CATH Clusters

Superfamily BPG-independent phosphoglycerate mutase, domain B
Functional Family

Enzyme Information

5.4.2.12
Phosphoglycerate mutase (2,3-diphosphoglycerate-independent).
based on mapping to UniProt G5EFZ1
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)

G5EFZ1
GPMI_CAEEL
Caenorhabditis elegans
2,3-bisphosphoglycerate-independent phosphoglycerate mutase

PDB Structure

PDB 5KGM
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases.
Yu, H., Dranchak, P., Li, Z., MacArthur, R., Munson, M.S., Mehzabeen, N., Baird, N.J., Battalie, K.P., Ross, D., Lovell, S., Carlow, C.K., Suga, H., Inglese, J.
Nat Commun