CATH Domain 1eqjA02
|3.40.720||Alkaline Phosphatase, subunit A|
|3.40.720.10||Alkaline Phosphatase, subunit A|
|Superfamily||Alkaline Phosphatase, subunit A|
|Functional Family||2,3-bisphosphoglycerate-independent phosphoglycerate mutase|
Phosphoglycerate mutase (2,3-diphosphoglycerate-independent).
based on mapping to UniProt Q9X519
2-phospho-D-glycerate = 3-phospho-D-glycerate.
-!- The enzymes from higher plants, algae, some fungi, nematodes, sponges, coelenterates, myriapods, arachnids, echinoderms, archaea and some bacteria (particularly Gram-positive) have maximum activity in the absence of 2,3-bisphospho-D-glycerate. -!- Cf. EC 18.104.22.168. -!- The reaction involves a phosphotransferase reaction to serine followed by transfer back to the glycerate at the other position. -!- Both metal ions are involved in the reaction. -!- Formerly EC 22.214.171.124 and EC 126.96.36.199.
UniProtKB Entries (1)
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate.