A0A0Q5AGS5 · A0A0Q5AGS5_9MICO
- ProteinBifunctional protein GlmU
- GeneglmU
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids490 (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 | 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 | 109 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 146 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 161 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 176 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 234 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 234 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 339 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 357 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 369 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 372 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 383 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 386 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 392-393 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: NY | ||||||
Binding site | 411 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 429 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Rathayibacter
Accessions
- Primary accessionA0A0Q5AGS5
Proteomes
Subcellular Location
Interaction
Subunit
Homotrimer.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-236 | Pyrophosphorylase | ||||
Sequence: MVDSTLAVVILAAGQGTRMKSRTPKVLHRLAGRPLLGHVLDTASSLDAAHVVTVVRHERERVAEAVLEHTPAALVVDQDDVPGTGRAVELGLAALPDDFDGTVVVLSADVPLLDAPTLRRLVDEHLVAANALTMLSCVLEDPTGFGRIVRAVDGGFASIVEQKDASDDELALTETNAGVYAFDAAALRSVIGAIGTDNAQREKYLTDAAAALKAAGRAIEAVPVQDRWLVAGINDR | ||||||
Domain | 8-126 | MobA-like NTP transferase | ||||
Sequence: VVILAAGQGTRMKSRTPKVLHRLAGRPLLGHVLDTASSLDAAHVVTVVRHERERVAEAVLEHTPAALVVDQDDVPGTGRAVELGLAALPDDFDGTVVVLSADVPLLDAPTLRRLVDEHL | ||||||
Region | 237-257 | Linker | ||||
Sequence: AQLADAALELNARIVRRWQLE | ||||||
Region | 258-490 | N-acetyltransferase | ||||
Sequence: GVTIQDPATTWIDVDAVLSPDVEILPGTQIKGPTVIASGAIIGPDTTLDACEIGEDAVVKRSDATLAVIGARAQVGPFSYLRPGTVLGERGKIGTYVETKNATIGAGSKVPHLSYVGDATIGEESNIGAGSIFANYDGVSKAASIVGSHVRAGSHNVFVAPVRIGDGAYTGAGTVIRKDIPAGALGITVAPQRNMAGWVEAHRPGTASATAAEAAQASESEDSDLPTGGSGEL | ||||||
Region | 461-490 | Disordered | ||||
Sequence: PGTASATAAEAAQASESEDSDLPTGGSGEL | ||||||
Compositional bias | 468-482 | Polar residues | ||||
Sequence: AAEAAQASESEDSDL |
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
- Length490
- Mass (Da)50,568
- Last updated2016-01-20 v1
- Checksum1AC9C46A0C59C57F
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 468-482 | Polar residues | ||||
Sequence: AAEAAQASESEDSDL |
Keywords
- Technical term