Phosphoglycerate mutase, 2,3-bisphosphoglycerate-independent (IPR005995)

Short name: Pgm_bpd_ind

Overlapping homologous superfamilies

Family relationships



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 [PMID: 7896694], Bacillus subtilis [PMID: 8021172], Bacillus stearothermophilus [PMID: 10388626], maize [PMID: 1535626], castor bean [PMID: 8260624], and Trypanosoma brucei [PMID: 10691985]. The structure of the B. stearothermophilus enzyme has two domains [PMID: 10764795]. 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.

GO terms

Biological Process

GO:0006007 glucose catabolic process

Molecular Function

GO:0004619 phosphoglycerate mutase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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