Difference between revisions of "Phosphatase Fold HP"

Revision as of 18:43, 1 January 2015

Phosphatase Classification: Fold PGM

PGM is short for PhosphoGlycerate Mutase. It can be classified as below [1, 2]:

• Monophosphoglycerate mutase (mPGM) - catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA)
  • dependent on 23PGA as a cofactor (dPGM) - found in animal, fungi, and bacteria
  • independent of 23PGA as a cofactor (iPGM) - found in plants, and bacteria
• Bisphosphoglycerate mutase (bPGM) - catalyzes primarily the interconversion of 1,3-phosphoglycerate (13PGA) and 23PGA

SCOP

The fold corresponds to SCOP fold phosphoglycerate mutase-like (c.60). It contains single superfamily, which include the families below:

• c.60.1.1: Cofactor-dependent phosphoglycerate mutase
• c.60.1.2: Histidine acid phosphatase
• c.60.1.4: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain

c60.1.1 and c60.1.4 forms dPGM.

Pfam

The fold PGM corresponds to histidine phosphatase superfamily in Pfam database. It contains two families: branch 1 and branch 2. Branch 1 includes dPGMs (corresponding to SCOP c60.1.1 + c60.1.4), branch 2 includes histidine acid phosphatase (corresponding to SCOP c60.1.2).

References

1. Jedrzejas MJ. Structure, function, and evolution of phosphoglycerate mutases: comparison with fructose-2,6-bisphosphatase, acid phosphatase, and alkaline phosphatase. Prog Biophys Mol Biol. 2000;73(2-4):263-87. DOI:10.1016/s0079-6107(00)00007-9 | PubMed ID:10958932 | HubMed [jedrzejas00]
2. Rigden DJ, Bagyan I, Lamani E, Setlow P, and Jedrzejas MJ. A cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus is actually a broad specificity phosphatase. Protein Sci. 2001 Sep;10(9):1835-46. DOI:10.1110/ps.15701 | PubMed ID:11514674 | HubMed [rigden01]