Phosphoglucosamine mutase, bacterial type (IPR006352)

Short name: GlmM_bact

Overlapping homologous superfamilies

Family relationships


The alpha-D-phosphohexomutase superfamily is composed of four related enzymes, each of which catalyses a phosphoryl transfer on their sugar substrates: phosphoglucomutase (PGM), phosphoglucomutase/phosphomannomutase (PGM/PMM), phosphoglucosamine mutase (PNGM), and phosphoacetylglucosamine mutase (PAGM) [PMID: 10506283]. PGM (EC: converts D-glucose 1-phosphate into D-glucose 6-phosphate, and participates in both the breakdown and synthesis of glucose [PMID: 15299905]. PGM/PMM (EC:; EC: are primarily bacterial enzymes that use either glucose or mannose as substrate, participating in the biosynthesis of a variety of carbohydrates such as lipopolysaccharides and alginate [PMID: 16595672, PMID: 14725765]. Both PNGM (EC: and PAGM (EC: are involved in the biosynthesis of UDP-N-acetylglucosamine [PMID: 10913078, PMID: 11004509].

Despite differences in substrate specificity, these enzymes share a similar catalytic mechanism, converting 1-phospho-sugars to 6-phospho-sugars via a biphosphorylated 1,6-phospho-sugar. The active enzyme is phosphorylated at a conserved serine residue and binds one magnesium ion; residues around the active site serine are well conserved among family members. The reaction mechanism involves phosphoryl transfer from the phosphoserine to the substrate to create a biophosphorylated sugar, followed by a phosphoryl transfer from the substrate back to the enzyme [PMID: 15238632].

The structures of PGM and PGM/PMM have been determined, and were found to be very similar in topology. These enzymes are both composed of four domains and a large central active site cleft, where each domain contains residues essential for catalysis and/or substrate recognition. Domain I contains the catalytic phosphoserine, domain II contains a metal-binding loop to coordinate the magnesium ion, domain III contains the sugar-binding loop that recognises the two different binding orientations of the 1- and 6-phospho-sugars, and domain IV contains a phosphate-binding site required for orienting the incoming phospho-sugar substrate.

This family describes GlmM, phosphoglucosamine mutase, also designated MrsA and YhbF in Escherichia coli [PMID: 8550580], UreC in Helicobacter pylori[PMID: 9171391], and femR315 or FemD in Staphylococcus aureus[PMID: 9286983]. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides.

In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. [PMID: 10671448, PMID: 10231382, PMID: 15720398, PMID: 10506283, PMID: 9549096, PMID: 15238632, PMID: 10913078, PMID: 12604356].

GO terms

Biological Process

GO:0005975 carbohydrate metabolic process

Molecular Function

GO:0000287 magnesium ion binding
GO:0008966 phosphoglucosamine mutase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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