2,3-bisphosphoglycerate-independent phosphoglycerate mutase, prokaryotes (IPR023665)

Short name: ApgAM_prokaryotes

Overlapping homologous superfamilies


Family relationships


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 [PMID: 17576516]. 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) [PMID: 12062435, PMID: 12076796], Pyrococcus furiosus [PMID: 12076796], and Sulfolobus solfataricus [PMID: 12644480]. These proteins were initially misidentified as phosphonopyruvate decarboxylase.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0046537 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.