A0A934TQ13 · A0A934TQ13_9BURK

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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
IDPosition(s)Description
Binding site23UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site81UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site86-87UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site110Mg2+ (UniProtKB | ChEBI)
Binding site145UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site159UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site232Mg2+ (UniProtKB | ChEBI)
Binding site232UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site342UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site360UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site372Proton acceptor
Binding site375UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site386UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site389acetyl-CoA (UniProtKB | ChEBI)
Binding site395-396acetyl-CoA (UniProtKB | ChEBI)
Binding site414acetyl-CoA (UniProtKB | ChEBI)
Binding site432acetyl-CoA (UniProtKB | ChEBI)
Binding site449acetyl-CoA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionglucosamine-1-phosphate N-acetyltransferase activity
Molecular Functionmagnesium ion binding
Molecular FunctionUDP-N-acetylglucosamine diphosphorylase activity
Biological Processcell morphogenesis
Biological Processcell wall organization
Biological Processlipid A biosynthetic process
Biological Processpeptidoglycan biosynthetic process
Biological Processregulation of cell shape
Biological ProcessUDP-N-acetylglucosamine biosynthetic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional protein GlmU

Including 2 domains:

  • Recommended name
    UDP-N-acetylglucosamine pyrophosphorylase
  • EC number
  • Alternative names
    • N-acetylglucosamine-1-phosphate uridyltransferase
  • Recommended name
    Glucosamine-1-phosphate N-acetyltransferase
  • EC number

Gene names

    • Name
      glmU
    • ORF names
      JJB11_01975

Organism names

  • Taxonomic identifier
  • Strain
    • KACC 17527
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Ramlibacter

Accessions

  • Primary accession
    A0A934TQ13

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-234Pyrophosphorylase
Domain6-135MobA-like NTP transferase
Region235-255Linker
Region256-467N-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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    467
  • Mass (Da)
    49,473
  • Last updated
    2023-02-22 v1
  • Checksum
    942F1F03EA59EC07
MTAVDVVVMAAGKGTRMKSRTAKVLHRLGGRPLIAHVMDTAHALAARRTIVITGHGAEDVEGWLRSAAAAQGRPSPDFVRQEPQLGTGHAVQQAVPVLPDDGIALILNGDVPLIRPETLQALVDKCGGERLALLTVEMADPTGYGRILRRGDAVQAIVEHKDASAAQRGIREVYTGFMAVPERKLKTWLARLSNDNAQREYYLTDIVQFAVADGCEVVASPAAEQVEVDGVNSPLQLAALERAFQSRQANALMEQGVRLADPARFDLRGRLSCGQDVEIDVNCVFQGEVSLGDNVRIGPNCVISNAKIAANVVLQAYTHIEGEEAGVEIGEGALIGPFARLRPGAQLGPEVHIGNFVEVKNSTLARGAKANHLAYLGDTTVGERVNYGAGSITANYDGANKNRTVIEADVHVGSNCVLVAPVTVAKGGTIGAGSVVNKNTEPGALTVARAKQVSITNWQRPKKAAKK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAEPWM010000001
EMBL· GenBank· DDBJ
MBK6004846.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help