S9SB63 · S9SB63_9RHOB
- ProteinBifunctional protein GlmU
- GeneglmU
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1087 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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
- D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
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) | ||||
Sequence: LAAG | ||||||
Binding site | 25 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 78 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 83-84 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: GT | ||||||
Binding site | 106-108 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: YGD | ||||||
Binding site | 108 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 144 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 159 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 174 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 231 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 231 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 320 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 338 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 350 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 353 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 364 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 367 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 373-374 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: NY | ||||||
Binding site | 392 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 410 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 427 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | carbohydrate derivative binding | |
Molecular Function | glucosamine-1-phosphate N-acetyltransferase activity | |
Molecular Function | glutamine-fructose-6-phosphate transaminase (isomerizing) activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | UDP-N-acetylglucosamine diphosphorylase activity | |
Biological Process | cell morphogenesis | |
Biological Process | cell wall organization | |
Biological Process | fructose 6-phosphate metabolic process | |
Biological Process | glutamine metabolic process | |
Biological Process | lipid A biosynthetic process | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | protein N-linked glycosylation | |
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 > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Rubellimicrobium
Accessions
- Primary accessionS9SB63
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-233 | Pyrophosphorylase | ||||
Sequence: MEGTGIAVVILAAGAGTRMESDRPKVLHELGGAPLLHHAMRTAAAIGPERVVVVTGVGAEAVEAAARAFDPDAVCVRQAEQLGTAHAVQQAAAALADHGGDVLVLYGDTPFVRPETIEAMQQARARADIVVLGFETADPQARYGRLVTDEGDGLLGIVEWKDADAATRAIRLCNSGVLLAEGAFLFALLREVDRANAAGEYYLTDVVALARGRGLRATVVRCEEAETLGVNSR | ||||||
Region | 234-254 | Linker | ||||
Sequence: AELRAAEAALQARMRAQALED | ||||||
Region | 255-1087 | N-acetyltransferase | ||||
Sequence: GVSMPLPETVVFAYDTVVGRDAVIESHVVFGPGVTVESGARIRAFSHLEGCHVSRGAIVGPFARLRPGAELAEAVHVGNFVEVKAAVLHEGVKVNHLSYVGDAEVGERTNIGAGTITCNYDGVSKHRTVIGREAFIGSDTMLVAPVRLGDGAVTASGSVITEDVPAGALALGRARQVVKPGLGARLMERLRAAKAARTKAPPGTGTGTGTGTGTGTGTGTGNDDGRGGLMCGIVGILGRHEVAPLLVEALRRLEYRGYDSAGVATVHEGRLDRRRAVGKLVNLSDLLVHAPLPGRSGIGHTRWATHGGPVEANAHPHRAGRVCVVHNGIIENFRELRAWAATQGLATESETDSEMVAVLCDHFLARGASPAEAVDRTLERVTGAYALAFLFEGEEDLLIVARKGSPLAIGHGEGEMFVGSDALALAPLTDRITYLEDGDRAVITRAGAEIRDAAGRPVSRPIRRIALDAVQVDKAGHRHFMAKEIAEQPGRLQDVLSHYLGEGGVRLPEGLDFRDYDRVTMVACGTAAYACQVARYWFEQVARLPAEVDVASEFRYRERPCHRGRWRCSSASRARRPTRWQRCATAGGGRRGRWRWSMWPNPPSPGRRTWCCRSWQGGRSASPRPRPLPVSLRFWGFWRCGRPRIAGRCPPPPMRRRWRRCRCCRASSTGRWTSRGRRGASPPIWPRRATSCSWGRGRMYPLALEGALKLKEISYIHAEGHASGELKHGPIALVDPLVPVIVLAPRDELFEKSVSNMQEVMARGGRVLLVTDRAGAQEAGEGVWETLVMPEIAPLWAPILYAVPAQLLAYHTAVAKGTDVDQPRNLAKSVTVE | ||||||
Region | 449-478 | Disordered | ||||
Sequence: AARTKAPPGTGTGTGTGTGTGTGTGTGNDD | ||||||
Compositional bias | 457-475 | Polar residues | ||||
Sequence: GTGTGTGTGTGTGTGTGTG | ||||||
Domain | 485-700 | Glutamine amidotransferase type-2 | ||||
Sequence: CGIVGILGRHEVAPLLVEALRRLEYRGYDSAGVATVHEGRLDRRRAVGKLVNLSDLLVHAPLPGRSGIGHTRWATHGGPVEANAHPHRAGRVCVVHNGIIENFRELRAWAATQGLATESETDSEMVAVLCDHFLARGASPAEAVDRTLERVTGAYALAFLFEGEEDLLIVARKGSPLAIGHGEGEMFVGSDALALAPLTDRITYLEDGDRAVITRA | ||||||
Domain | 949-1077 | SIS | ||||
Sequence: GRGRMYPLALEGALKLKEISYIHAEGHASGELKHGPIALVDPLVPVIVLAPRDELFEKSVSNMQEVMARGGRVLLVTDRAGAQEAGEGVWETLVMPEIAPLWAPILYAVPAQLLAYHTAVAKGTDVDQP |
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
- Length1,087
- Mass (Da)116,697
- Last updated2013-10-16 v1
- Checksum9C8C4830DE4338D9
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 457-475 | Polar residues | ||||
Sequence: GTGTGTGTGTGTGTGTGTG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AOLV01000008 EMBL· GenBank· DDBJ | EPX87370.1 EMBL· GenBank· DDBJ | Genomic DNA |