Difference between revisions of "Phosphatase Fold HP"
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* Bisphosphoglycerate mutase (bPGM) - catalyzes primarily the interconversion of 1,3-phosphoglycerate (13PGA) and 23PGA | * Bisphosphoglycerate mutase (bPGM) - catalyzes primarily the interconversion of 1,3-phosphoglycerate (13PGA) and 23PGA | ||
| − | === [[Phosphatase_Glossary#SCOP|SCOP]] === | + | ==== [[Phosphatase_Glossary#SCOP|SCOP]] ==== |
| − | The fold corresponds to SCOP fold phosphoglycerate mutase (c.60 | + | The fold corresponds to SCOP fold [http://scop.berkeley.edu/sunid=53253 phosphoglycerate mutase-like (c.60)]. It contains single superfamily, which include the families below: |
* c.60.1.1: Cofactor-dependent phosphoglycerate mutase | * c.60.1.1: Cofactor-dependent phosphoglycerate mutase | ||
* c.60.1.2: Histidine acid phosphatase | * c.60.1.2: Histidine acid phosphatase | ||
* c.60.1.4: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain | * c.60.1.4: 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, phosphatase domain | ||
| + | |||
c60.1.1 and c60.1.4 forms dPGM. | c60.1.1 and c60.1.4 forms dPGM. | ||
Revision as of 18:39, 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
dPGM is also known as histidine phosphatase, branch 1.
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 |
