| Type: | Family | Name: | Phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent |
| Description: | This 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM) is a metalloenzyme found particularly in eubacteria and higher plants. It is distantly related to archaeal iPGAM () and distinct from the unrelated cofactor-dependent PGAM (). Activity has been demonstrated for proteins from a variety of organisms, including Pseudomonas syringae pv. tomato[], Bacillus subtilis[], Bacillus stearothermophilus[], maize [], castor bean [], and Trypanosoma brucei[]. The structure of the B. stearothermophilus enzyme has two domains []. Residues 1-76 and 311-511 form the phosphatase domain, containing the active site residue and two metal-binding sites. This domain is similar to alkaline phosphatase and arylsulphatase, which are members of the SCOP alkaline phosphatase-like superfamily, but there is meagre sequence similarity outside of the metal-binding segments. Residues 77-310 form the phosphotransferase domain, which is poorly conserved (or perhaps unrelated) in the archaeal enzymes. | Short Name: | Pgm_bpd_ind |
