| General Information |
| MoonProt ID | 447 |
| First appeared in release | 4.0 |
| Name(s) | N-acetylglucosamine 1-phosphate uridyltransferase |
| UniProt ID | Q2FJE2 |
| GO terms | "GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0003977 UDP-N-acetylglucosamine diphosphorylase activity
GO:0016740 transferase activity
GO:0016746 acyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
GO:0000902 cell morphogenesis
GO:0006048 UDP-N-acetylglucosamine biosynthetic process
GO:0008360 regulation of cell shape
GO:0009245 lipid A biosynthetic process
GO:0009252 peptidoglycan biosynthetic process
GO:0071555 cell wall organization
GO:0005737 cytoplasm
GO:0016020 membrane" |
| Organisms for which functions have been demonstrated | Staphylococcus aureus (strain USA300) |
| Sequence length | 450.0 |
| FASTA sequence | >sp|Q2FJE2|GLMU_STAA3 Bifunctional protein GlmU OS=Staphylococcus aureus (strain USA300) OX=367830 GN=glmU PE=3 SV=1 MRRHAIILAAGKGTRMKSKKYKVLHEVAGKPMVEHVLESVKGSGVDQVVTIVGHGAESVK GHLGERSLYSFQEEQLGTAHAVQMAKSHLEDKEGTTIVVCGDTPLITKETLETLIAHHED ANAQATVLSASIQQPYGYGRIVRNASGRLERIVEEKDATQAEKDINEISSGIFAFNNKTL FEKLTQVKNDNAQGEYYLPDVLSLILNDGGIVEVYRTNDVEEIMGVNDRVMLSQAEKAMQ RRTNHYHMLNGVTIIDPDSTYIGPDVTIGSDTVIEPGVRINGRTEIGEDVVIGQYSEINN STIENGACIQQSVVNDASVGANTKVGPFAQLRPGAQLGADVKVGNFVEIKKADLKDGAKV SHLSYIGDAVIGERTNIGCGTITVNYDGENKFKTIVGKDSFVGCNVNLVAPVTIGDDVLV AAGSTITDDVPNDSLAVARARQTTKEGYRK |
| Structure Information |
| PDB ID | NA |
| Quaternary structure | homotrimer |
| SCOP | NA |
| CATH | NA |
| TM Helix Prediction | not TM helices |
| DisProt Annotation | not in DisProt |
| Predicted Disorder Regions | Predicted disorder at N terminus (aa 1-10) and C terminus (aa 440-450) |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | enzyme,uridyltransferase activity of GlmU catalyzes the Mg2+-dependent reaction of UTP with GlcNAc 1-P to form UDP-GlcNAc and pyrophosphate. |
| References for function | Pederick JL, Kumar A, Pukala TL, Bruning JB. Functional and structural characterization of Staphylococcus aureus N-acetylglucosamine 1-phosphate uridyltransferase (GlmU) reveals a redox-sensitive acetyltransferase activity. Protein Sci. 2025 Apr;34(4):e70111. doi: 10.1002/pro.70111. PMID: 40143772; PMCID: PMC11947611. |
| E.C. number | EC:2.3.1.157 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | enzyme, acetyltransferase catalyzing the reaction of acetyl coenzyme A (AcCoA) and GlcN 1-P to form CoA and N-acetylglucosamine 1-phosphate (GlcNAc 1-P). |
| References for function | Pederick JL, Kumar A, Pukala TL, Bruning JB. Functional and structural characterization of Staphylococcus aureus N-acetylglucosamine 1-phosphate uridyltransferase (GlmU) reveals a redox-sensitive acetyltransferase activity. Protein Sci. 2025 Apr;34(4):e70111. doi: 10.1002/pro.70111. PMID: 40143772; PMCID: PMC11947611. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |