InterPro domain: IPR004456

This family represents 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM), it is a metalloenzyme found particularly in archaea and some eubacteria. It is responsible for the interconversion of 2-phosphoglycerate and 3-phosphoglycerate [ 1 ]. It is distantly related to the iPGAM ( IPR005995 ) 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) [ 2 , 3 ], Pyrococcus furiosus [ 4 ], and Sulfolobus solfataricus [ 4 ]. These proteins were initially misidentified as phosphonopyruvate decarboxylase.

1. Characterization of cofactor-dependent and cofactor-independent phosphoglycerate mutases from Archaea. Extremophiles 11, 647-57
2. A divergent archaeal member of the alkaline phosphatase binuclear metalloenzyme superfamily has phosphoglycerate mutase activity. FEBS Lett. 517, 190-4
3. Molecular characterization of phosphoglycerate mutase in archaea. FEMS Microbiol. Lett. 212, 111-20
4. Phosphoprotein with phosphoglycerate mutase activity from the archaeon Sulfolobus solfataricus. J. Bacteriol. 185, 2112-21