A0A1J4SSH9 · A0A1J4SSH9_9BACT
- ProteinBifunctional protein GlmU
- GeneglmU
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids458 (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
- N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H+ = UDP-N-acetyl-alpha-D-glucosamine + diphosphate
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
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.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 11-14 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 25 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 75 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 80-81 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 106 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 142 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 157 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 174 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 232 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 232 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 338 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 356 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Active site | 368 | Proton acceptor | |||
Binding site | 371 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 382 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 385 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 391-392 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 410 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 428 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 445 | 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 > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae
Accessions
- Primary accessionA0A1J4SSH9
Proteomes
Subcellular Location
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-234 | Pyrophosphorylase | |||
Domain | 8-133 | MobA-like NTP transferase | |||
Region | 235-255 | Linker | |||
Region | 256-458 | N-acetyltransferase | |||
Sequence similarities
In the C-terminal section; belongs to the transferase hexapeptide repeat family.
In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length458
- Mass (Da)46,903
- Last updated2017-02-15 v1
- MD5 ChecksumECC398F2814648F6B74A867F46609519
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MNUQ01000121 EMBL· GenBank· DDBJ | OIO00975.1 EMBL· GenBank· DDBJ | Genomic DNA |