A0A6B8W4J3 · A0A6B8W4J3_9CORY

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.

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 site13-16UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site27UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site84UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site89-90UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site114Mg2+ (UniProtKB | ChEBI)
Binding site151UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site166UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site181UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site239Mg2+ (UniProtKB | ChEBI)
Binding site239UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site344UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site362UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site374Proton acceptor
Binding site377UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site388UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site391acetyl-CoA (UniProtKB | ChEBI)
Binding site397-398acetyl-CoA (UniProtKB | ChEBI)
Binding site416acetyl-CoA (UniProtKB | ChEBI)
Binding site434acetyl-CoA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmembrane
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
      COCCU_04495

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 2039
  • Taxonomic lineage
    Bacteria > Bacillati > Actinomycetota > Actinomycetes > Mycobacteriales > Corynebacteriaceae > Corynebacterium

Accessions

  • Primary accession
    A0A6B8W4J3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-241Pyrophosphorylase
Domain11-143MobA-like NTP transferase
Region242-262Linker
Region263-488N-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
    488
  • Mass (Da)
    50,978
  • Last updated
    2020-06-17 v1
  • MD5 Checksum
    A9E93E20C82C674913779015C2476F09
MSTSPNPCALVVLAAGAGTRMKSETQKTLHEIGGRSLLSHSLHAAAGVSPEHIVAVIGHKREQVGPAVEAVAEQLNREVLTAIQEEQNGTGHAVQCGLAPLPDFEGTIIVTNADVPLLRPETLGQLLEAHTAVPTAVTVLTMRLEDPTGYGRIIRNAEGEVTAIVEQKDATEEQRNVDEVNSGVFAFDAAVLRDALGKLDSDNAQGELYLTDVLGIAREAGHPVRAFLAADPAELAGVNNRVQLAEAGRELNRRTVETAMLGGATIIDPESTWIGVDVQVGRDVVIHPGTQLWGTTSIADNAEIGPDTTLRDMTIGTGATVIRTHGESSVIGAHASVGPFTYIRPNTVLGEDGKLGGFVEAKNAQIGRGSKVPHLTYVGDATIGEESNIGASSVFVNYDGVTKHHTTIGSHVRTGSDTMFIAPVTVGDGAYSGAGTVIKEDVPPGALAVSGGSQRNLEGWVQKKRPGTPAAEAAERALADFSELNQEG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP046455
EMBL· GenBank· DDBJ
QGU06847.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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