CATH Domain 1o98A02

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.40	3-Layer(aba) Sandwich
	3.40.720	Alkaline Phosphatase, subunit A
	3.40.720.10	Alkaline Phosphatase, subunit A

Domain Context

CATH Clusters

Superfamily	Alkaline Phosphatase, subunit A
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 Q9X519

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)

Q9X519

GPMI_GEOSE

Geobacillus stearothermophilus

2,3-bisphosphoglycerate-independent phosphoglycerate mutase

PDB Structure

PDB	1O98
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Insights Into the Catalytic Mechanism of Cofactor-Independent Phosphoglycerate Mutase from X-Ray Crystallography, Simulated Dynamics and Molecular Modeling Rigden, D.J., Mello, L.V., Lamani, E., Littlejohn, J.E., Jedrzejas, M.J. J.Mol.Biol.