Protein Domain : IPR006352

Type:  Family Name:  Phosphoglucosamine mutase, bacterial type
Description:  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) []. PGM () converts D-glucose 1-phosphate into D-glucose 6-phosphate, and participates in both the breakdown and synthesis of glucose []. PGM/PMM (; ) 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 [, ]. Both PNGM () and PAGM () are involved in the biosynthesis of UDP-N-acetylglucosamine [, ]. 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 [].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[], UreC in Helicobacter pylori[], and femR315 or FemD in Staphylococcus aureus[]. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides. Short Name:  GlmM_bact
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0 Child Features

6 Contains

DB identifier Type Name
IPR005844 Domain Alpha-D-phosphohexomutase, alpha/beta/alpha domain I
IPR005845 Domain Alpha-D-phosphohexomutase, alpha/beta/alpha domain II
IPR005843 Domain Alpha-D-phosphohexomutase, C-terminal
IPR005846 Domain Alpha-D-phosphohexomutase, alpha/beta/alpha domain III
IPR016055 Domain Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III
IPR016066 Conserved_site Alpha-D-phosphohexomutase, conserved site

2 Cross Referencess

Identifier
TIGR01455
MF_01554_B

0 Found In

3 GO Annotations

GO Term Gene Name
GO:0000287 IPR006352
GO:0008966 IPR006352
GO:0005975 IPR006352

3 Ontology Annotations

GO Term Gene Name
GO:0000287 IPR006352
GO:0008966 IPR006352
GO:0005975 IPR006352

1 Parent Features

DB identifier Type Name
IPR005841 Family Alpha-D-phosphohexomutase superfamily

4 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Araha.11756s0097.1.p PAC:28856584 Arabidopsis halleri 444  
Brdisv1pangenome1008974m.p PAC:33624102 Brachypodium distachyon Pangenome 352  
Brdisv1pangenome1009410m.p PAC:33622762 Brachypodium distachyon Pangenome 328  
Brdisv1BdTR11A1046343m.p PAC:35690580 Brachypodium distachyon BdTR11a 328  

10 Publications

First Author Title Year Journal Volume Pages PubMed ID
            14725765
            15299905
            16595672
            10506283
            10913078
            11004509
            15238632
            8550580
            9171391
            9286983