Difference between revisions of "Phosphatase Fold HP"

Revision as of 18:56, 1 January 2015

Phosphatase Classification: Fold PGM

PGM is short for PhosphoGlycerate Mutase. Traditionally, PGMs are 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

The name: PGM vs histidine phosphatase

All of these new discoveries have been phosphatase activities of one kind or another, illustrating that, ironically enough, the earliest and arguably best studied member of the superfamily is anomalous in catalysing primarily a mutase

a reading of the literature also illustrates a disadvantage arising from the mutase-dominated superfamily history; many superfamily members discovered in genomes have been suggested to be mutases when a phosphatase activity is in fact much more likely.

PGM corresponds to histidine phosphatase superfamily in Pfam database. It contains two families: branch 1 and branch 2. Branch 1 includes dPGMs, branch 2 includes histidine acid phosphatase.

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.

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]