CATH Domain 2ifyA02

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.40	3-Layer(aba) Sandwich
	3.40.1450	2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain
	3.40.1450.10	BPG-independent phosphoglycerate mutase, domain B

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	PDBSum Proteopedia
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.