CATH Classification

Domain Context

CATH Clusters

Superfamily Phosphoglycerate mutase-like
Functional Family 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Enzyme Information
Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent).
based on mapping to UniProt P36623
2-phospho-D-glycerate = 3-phospho-D-glycerate.
-!- The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, some fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. -!- The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His(10) in man and Escherichia coli, His(8) in Saccharomyces cerevisiae). -!- This phosphate can be transferred to the free OH of 2-phospho-D- glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. -!- Cf. EC -!- The enzyme has no requirement for metal ions. -!- This enzyme also catalyze, slowly, the reactions of EC -!- Formerly EC and EC

UniProtKB Entries (1)

Schizosaccharomyces pombe 972h-
Phosphoglycerate mutase

PDB Structure

External Links
Organism Saccharomyces
Primary Citation
Solution structure and dynamics of an open beta-sheet, glycolytic enzyme, monomeric 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe.
Uhrinova, S., Uhrin, D., Nairn, J., Price, N.C., Fothergill-Gilmore, L.A., Barlow, P.N.