C1A333 · C1A333_RHOE4
- ProteinBifunctional protein GlmU
- GeneglmU
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids483 (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 | 8-11 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: LAAG | ||||||
Binding site | 22 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 79 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 84-85 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: GT | ||||||
Binding site | 110 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 148 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 163 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 178 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 236 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 236 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 341 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 359 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 371 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 374 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 385 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 388 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 394-395 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: NY | ||||||
Binding site | 413 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 431 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: A |
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 > Nocardiaceae > Rhodococcus > Rhodococcus erythropolis group
Accessions
- Primary accessionC1A333
Proteomes
Subcellular Location
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-238 | Pyrophosphorylase | ||||
Sequence: MQTAVIVLAAGAGTRMKSKTPKVLHTLAGRSMLAHSLHAATSLNPTHLVTVVGHDRERVTEAVNAVAGELGRPVTVAVQDEQKGTGHAVSCGLEGLPADFAGTVLVTAADVPLLDGKTIADLLAQHTAAPAAAVTVLTSTALDPTGYGRILRTTDGEVNAIVEEKEATDSQRSITEVNSGVYAFDFETLRDALASLDSNNAQHEFYLTDVIMIARRAGKRVRAQHIADSVLVAGANDR | ||||||
Domain | 5-147 | MobA-like NTP transferase | ||||
Sequence: VIVLAAGAGTRMKSKTPKVLHTLAGRSMLAHSLHAATSLNPTHLVTVVGHDRERVTEAVNAVAGELGRPVTVAVQDEQKGTGHAVSCGLEGLPADFAGTVLVTAADVPLLDGKTIADLLAQHTAAPAAAVTVLTSTALDPTGY | ||||||
Region | 239-259 | Linker | ||||
Sequence: VQLSTLAREMNRRILETWMRA | ||||||
Region | 260-483 | N-acetyltransferase | ||||
Sequence: GVTVVDPASTWIDCGVHIAQDVTLLPGVQLTGTTSVGEDAVIGPDTTLDNVSVGERAEVVRSHGTDSVIGADATVGPFAYLRPATRLGDHGKIGAYVETKNADIGEHSKIPHLTYVGDATIGHHSNIGASSVFVNYDGVNKSRTVVGSHVRTGSDTMFVAPLTVGDGAYTGAGTVLRNDVPPGALAVSGGLQRNIEGWVQKNRPGTPAADAAAAAAQPDGPATT | ||||||
Region | 460-483 | Disordered | ||||
Sequence: KNRPGTPAADAAAAAAQPDGPATT |
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
- Length483
- Mass (Da)50,188
- Last updated2009-05-26 v1
- Checksum43D9A351824E9E42
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP008957 EMBL· GenBank· DDBJ | BAH35018.1 EMBL· GenBank· DDBJ | Genomic DNA |