A0A3S4KW49 · A0A3S4KW49_AVIVO
- ProteinBifunctional protein GlmU
- GeneglmU
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids456 (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
- H+ + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
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 | 9-12 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: LAAG | ||||||
Binding site | 23 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 74 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 79-80 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: GT | ||||||
Binding site | 101-103 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: YGD | ||||||
Binding site | 103 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 138 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 152 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 167 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 225 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 225 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 331 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 349 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 361 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 364 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 375 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 378 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 384-385 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: NY | ||||||
Binding site | 403 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 421 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 438 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: R |
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 > Pseudomonadota > Gammaproteobacteria > Pasteurellales > Pasteurellaceae > Avibacterium
Accessions
- Primary accessionA0A3S4KW49
Proteomes
Subcellular Location
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-227 | Pyrophosphorylase | ||||
Sequence: MKNLSVVILAAGKGTRMYSDLPKVLHKVAGKPMVKHVIDTAKQLNADNIHLIYGHGAELLQQHLADENVNWVLQPVQLGTGHAMQQAAPFFADDENIVMLYGDAPLITAQTLQKLIDAKPENGIALLTAHLDDPTGYGRIIRQDGNVVAIVEQKDATPEQLAIQEVNTGVMVSSGASFRKWLAKLDNNNAQGEYYMTDVIKFANQDGCKVAAVQAQDLMEVEGANNR | ||||||
Domain | 6-126 | MobA-like NTP transferase | ||||
Sequence: VVILAAGKGTRMYSDLPKVLHKVAGKPMVKHVIDTAKQLNADNIHLIYGHGAELLQQHLADENVNWVLQPVQLGTGHAMQQAAPFFADDENIVMLYGDAPLITAQTLQKLIDAKPENGIAL | ||||||
Region | 228-248 | Linker | ||||
Sequence: LQLAELERYYQRKQAEKLLLA | ||||||
Region | 249-456 | N-acetyltransferase | ||||
Sequence: GVSLRDPSRFDLRGEILHGKDVEIDVNVIIEGNVKLGDRVKIGAGCIIKDCVIGDDVEIKPYSVFEDAVIGEQAQIGPFSRLRPGTELAAQTHIGNFVEVKKSHIGKGSKVNHLSYVGDSEIGANCNIGAGTITCNYDGVNKFKTVIGDDVFVGSDSQLVAPVTIAKGATIGAGTTVTKDIAENELVISRVPQRNIQGWKRPEKLEKK |
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
- Length456
- Mass (Da)49,532
- Last updated2019-04-10 v1
- Checksum4BCBD0F71BBCD704
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LR134167 EMBL· GenBank· DDBJ | VEB22381.1 EMBL· GenBank· DDBJ | Genomic DNA |