Phosphatase Fold HP

Phosphatase Classification: Fold HP

HP is short for histidine phosphatase, which is also known as phosphoglycerate mutase (PGM).

Naming: histidine phosphatase (HP) or phosphoglycerate mutase (PGM)

The earliest and arguably best studied members of this group of genes primarily function as mutase, which results in naming them PGM. However, most if not all of later discoveries have been phosphatase activities of one kind or another [1]. To reflect this fact, we call it histidine phosphatase rather than phosphoglycerate mutase, although the genes are sometimes referred as PGM in literature and SCOP database.

Classification

The fold/superfamily HP consists of two families based upon sequence similarity: branch 1 and branch 2 [1]. This classification is largely the same with Pfam classification.

Traditional classification

Traditionally, HP/PGM is classified as below [2, 3]:

• 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

Pfam

HP 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. Branch 1 is largely dPGM.

SCOP

HP 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. Rigden DJ. The histidine phosphatase superfamily: structure and function. Biochem J. 2008 Jan 15;409(2):333-48. DOI:10.1042/BJ20071097 |
2. 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 |
3. 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 |