InterPro domain: IPR005995

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 ( IPR004456 ) and distinct from the unrelated cofactor-dependent PGAM. Activity has been demonstrated for proteins from a variety of organisms, including Pseudomonas syringae pv. tomato [ 1 ], Bacillus subtilis [ 2 ], Bacillus stearothermophilus [ 3 ], maize [ 4 ], castor bean [ 5 ], and Trypanosoma brucei [ 6 ]. The structure of the B. stearothermophilus enzyme has two domains [ 7 ]. 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.

1. Isolation and sequence analysis of the Pseudomonas syringae pv. tomato gene encoding a 2,3-diphosphoglycerate-independent phosphoglyceromutase. J. Bacteriol. 177, 1727-33
2. Cloning and nucleotide sequences of the genes encoding triose phosphate isomerase, phosphoglycerate mutase, and enolase from Bacillus subtilis. J. Bacteriol. 176, 3903-10
3. Structural studies on a 2,3-diphosphoglycerate independent phosphoglycerate mutase from Bacillus stearothermophilus. J. Struct. Biol. 126, 156-65
4. Cloning and sequencing of a cDNA encoding 2,3-bisphosphoglycerate-independent phosphoglycerate mutase from maize. Possible relationship to the alkaline phosphatase family. J. Biol. Chem. 267, 12797-803
5. Higher-plant cofactor-independent phosphoglyceromutase: purification, molecular characterization and expression. Plant Mol. Biol. 23, 1039-53
6. Trypanosoma brucei contains a 2,3-bisphosphoglycerate independent phosphoglycerate mutase. Eur. J. Biochem. 267, 1464-72
7. Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate. J. Biol. Chem. 275, 23146-53