1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR004456 | Family | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase |
| Type: | Family | Name: | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, prokaryotes |
| Description: | This family represents 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from baceria and archaea. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase is a metalloenzyme found particularly in archaea and some eubacteria. It is responsble for the interconversion of 2-phosphoglycerate and 3-phosphoglycerate []. It is distantly related to the iPGAM () characteristic of plants and many eubacteria. The common active site and metal-binding residues of the phosphatase domain are easily identified, but the putative phosphotransferase domain is highly diverged. These proteins are unrelated to the cofactor-dependent PGAM (). Activity has been demonstrated for proteins from Methanocaldococcus jannaschii(Methanococcus jannaschii) [, ], Pyrococcus furiosus[], and Sulfolobus solfataricus[]. These proteins were initially misidentified as phosphonopyruvate decarboxylase. | Short Name: | ApgAM_prokaryotes |
| DB identifier | Type | Name |
|---|---|---|
| IPR004456 | Family | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase |
