Phosphatase Fold HP
From PhosphataseWiki
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
- 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 |
- 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 |