Difference between revisions of "Phosphatase Fold HP"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PGM|Fold PGM]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PGM|Fold PGM]] | ||
| − | PGM is short for PhosphoGlycerate Mutase. | + | PGM is short for PhosphoGlycerate Mutase. Traditionally, PGMs are classified as below <cite>jedrzejas00, rigden01</cite>: |
* Monophosphoglycerate mutase (mPGM) - catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA) | * Monophosphoglycerate mutase (mPGM) - catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA) | ||
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** independent of 23PGA as a cofactor (iPGM) - found in plants, 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 | * Bisphosphoglycerate mutase (bPGM) - catalyzes primarily the interconversion of 1,3-phosphoglycerate (13PGA) and 23PGA | ||
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| + | ===== 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 | ||
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| + | 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. | ||
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| + | PGM corresponds to [http://pfam.xfam.org/clan/CL0071 histidine phosphatase superfamily] in [[Phosphatase_Glossary#Pfam|Pfam database]]. It contains two families: [http://pfam.xfam.org/family/PF00300 branch 1] and [http://pfam.xfam.org/family/PF00328 branch 2]. Branch 1 includes dPGMs, branch 2 includes histidine acid phosphatase. | ||
===== [[Phosphatase_Glossary#SCOP|SCOP]] ===== | ===== [[Phosphatase_Glossary#SCOP|SCOP]] ===== | ||
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c60.1.1 and c60.1.4 forms dPGM. | c60.1.1 and c60.1.4 forms dPGM. | ||
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=== References === | === References === | ||
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
- 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 |
