A4QCS3 · GLMU_CORGB
- ProteinBifunctional protein GlmU
- GeneglmU
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids485 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic activity
- alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H+
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2.
Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 13-16 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 27 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 84 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 89-90 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 114 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 151 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 166 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 181 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 239 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 239 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 344 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 362 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Active site | 374 | Proton acceptor | |||
Binding site | 377 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 388 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 391 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 397-398 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 416 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 434 | acetyl-CoA (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | glucosamine-1-phosphate N-acetyltransferase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | UDP-N-acetylglucosamine diphosphorylase activity | |
Biological Process | cell morphogenesis | |
Biological Process | cell wall organization | |
Biological Process | lipid A biosynthetic process | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | regulation of cell shape | |
Biological Process | UDP-N-acetylglucosamine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional protein GlmU
Including 2 domains:
- Recommended nameUDP-N-acetylglucosamine pyrophosphorylase
- EC number
- Alternative names
- Recommended nameGlucosamine-1-phosphate N-acetyltransferase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Corynebacteriaceae > Corynebacterium
Accessions
- Primary accessionA4QCS3
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000337719 | 1-485 | Bifunctional protein GlmU | ||
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-241 | Pyrophosphorylase | |||
Region | 242-262 | Linker | |||
Region | 263-485 | N-acetyltransferase | |||
Region | 465-485 | Disordered | |||
Sequence similarities
In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
In the C-terminal section; belongs to the transferase hexapeptide repeat family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length485
- Mass (Da)50,544
- Last updated2007-05-15 v1
- MD5 ChecksumD43E6912CF7F241397AAE424847A3EEC
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP009044 EMBL· GenBank· DDBJ | BAF54020.1 EMBL· GenBank· DDBJ | Genomic DNA |