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A0A1X3EZD0 · A0A1X3EZD0_9BRAD

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 site11-14UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site25UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site78UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site83-84UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site108Mg2+ (UniProtKB | ChEBI)
Binding site144UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site158UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site173UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site230Mg2+ (UniProtKB | ChEBI)
Binding site230UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site319UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site337UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site349Proton acceptor
Binding site352UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site363UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site366acetyl-CoA (UniProtKB | ChEBI)
Binding site372-373acetyl-CoA (UniProtKB | ChEBI)
Binding site409acetyl-CoA (UniProtKB | ChEBI)
Binding site426acetyl-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

Enzyme and pathway databases

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
      BSZ18_22260
      , BSZ24_35005

Organism names

  • Taxonomic identifier
  • Strains
    • UBMA182
    • UBMA195
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Nitrobacteraceae > Bradyrhizobium

Accessions

  • Primary accession
    A0A1X3EZD0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-232Pyrophosphorylase
Domain9-136MobA-like NTP transferase
Region233-253Linker
Region254-451N-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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    451
  • Mass (Da)
    47,211
  • Last updated
    2017-07-05 v1
  • MD5 Checksum
    09EBF874235C6FDC0833675F05225B9C
MTARSSLTIVLAAGEGTRMRSHLPKVLHPVAHQSLLAHVLAAAPKGTGTSLAVVIGPDHQAVADEARRIRPDALTFVQQERLGTAHAVLAARDAIARGVDDLLIAFGDTPLISAETFARLRAPLAKGAAIAALGFRAADPTGYGRFIVEGDRLVAIREQADASAEERKIDLCNAGVMAIDGRRALAILDKIGNANSKGEYYLTDAVGIISEQGWDAVVIETSEDEVRGINTKAQLAEAEGVMQARLRKVAMESGVTLIAPETVYLAADTVFGKDVTIEPFVVIGPGVSIGDGTVVHSFSHIVETKLGKKVSIGPYARLRPGTSLGDGARIGNFVETKAATLEAGVKVNHLSYIGDAIIGANSNIGAGTITCNYDGFKKHKTIIGQGAFVGTNSSLVAPVTIGNGAYIGSGSVITRDVPDDAMALERSPQTIREGGAVRYRELKTGGKKPEK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NAFF01000113
EMBL· GenBank· DDBJ
OSI83144.1
EMBL· GenBank· DDBJ
Genomic DNA
NAFI01000179
EMBL· GenBank· DDBJ
OSJ06352.1
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.
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