CATH Classification

Domain Context

CATH Clusters

Superfamily Phosphoglycerate mutase-like
Functional Family Phosphoglycerate mutase 1

Enzyme Information

5.4.2.11
Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent).
based on mapping to UniProt P9WIC9
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 5.4.2.12. -!- The enzyme has no requirement for metal ions. -!- This enzyme also catalyze, slowly, the reactions of EC 5.4.2.4. -!- Formerly EC 2.7.5.3 and EC 5.4.2.1.

UniProtKB Entries (1)

P9WIC9
GPMA_MYCTU
Mycobacterium tuberculosis H37Rv
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

PDB Structure

PDB 1RII
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The 1.70 angstroms X-ray crystal structure of Mycobacterium tuberculosis phosphoglycerate mutase.
Muller, P., Sawaya, M.R., Pashkov, I., Chan, S., Nguyen, C., Wu, Y., Perry, L.J., Eisenberg, D.
Acta Crystallogr.,Sect.D