A0A840G1Y3 · A0A840G1Y3_RHOTE
- ProteinBifunctional protein GlmU
- GeneglmU
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids463 (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 | 76 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 81-82 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 107-109 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 109 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 143 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 158 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 173 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 231 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 231 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 337 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 355 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Active site | 367 | Proton acceptor | |||
Binding site | 370 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 381 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | |||
Binding site | 384 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 390-391 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 409 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 427 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 444 | 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 > Pseudomonadota > Betaproteobacteria > Rhodocyclales > Rhodocyclaceae > Rhodocyclus
Accessions
- Primary accessionA0A840G1Y3
Proteomes
Subcellular Location
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-233 | Pyrophosphorylase | |||
Domain | 9-128 | MobA-like NTP transferase | |||
Region | 234-254 | Linker | |||
Region | 255-463 | N-acetyltransferase | |||
Region | 427-463 | Disordered | |||
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
- Length463
- Mass (Da)48,642
- Last updated2021-09-29 v1
- Checksum90DFF7E57C007FED
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JACIGE010000001 EMBL· GenBank· DDBJ | MBB4245966.1 EMBL· GenBank· DDBJ | Genomic DNA |