A0A371IT09 · A0A371IT09_9FIRM
- ProteinBifunctional protein GlmU
- GeneglmU
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids457 (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 | 8-11 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 22 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 72 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 77-78 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 101 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 138 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 153 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 168 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 226 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 226 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 331 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 349 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Active site | 361 | Proton acceptor | |||
Binding site | 364 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 375 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 384-385 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 403 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 421 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 438 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Peptostreptococcales > Peptostreptococcaceae > Romboutsia
Accessions
- Primary accessionA0A371IT09
Proteomes
Subcellular Location
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-228 | Pyrophosphorylase | |||
Domain | 4-214 | Nucleotidyl transferase | |||
Region | 229-249 | Linker | |||
Region | 250-457 | 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
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length457
- Mass (Da)50,176
- Last updated2018-11-07 v1
- MD5 ChecksumD756222B5008A79E2EF2A1150FBCBD13
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NOJZ02000010 EMBL· GenBank· DDBJ | RDY23603.1 EMBL· GenBank· DDBJ | Genomic DNA |