U1MSN7 · U1MSN7_9MICO

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.

TypeIDPosition(s)Description
Binding site9-12UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site23UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site76UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site81-82UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site104-106UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site106Mg2+ (UniProtKB | ChEBI)
Binding site143UDP-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 site231Mg2+ (UniProtKB | ChEBI)
Binding site231UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site336UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site354UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site366Proton acceptor
Binding site369UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site380UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site383acetyl-CoA (UniProtKB | ChEBI)
Binding site389-390acetyl-CoA (UniProtKB | ChEBI)
Binding site408acetyl-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
      L332_10895

Organism names

  • Taxonomic identifier
  • Strain
    • RW1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Agrococcus

Accessions

  • Primary accession
    U1MSN7

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-233Pyrophosphorylase
Domain6-132MobA-like NTP transferase
Region234-254Linker
Region255-476N-acetyltransferase
Region451-476Disordered

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
    476
  • Mass (Da)
    49,780
  • Last updated
    2013-11-13 v1
  • Checksum
    5D19C284094822BD
MPSIAVIVLAAGAGTRMKSRTPKPLHPLAGKPLIAHVLSAAGELHPDRIVAVVRHERDRMAEAVLEFAPHVVIADQDEIPGTGRAVEQGLEALADFEGHVVVLSGDVPLIDADTLRALIERHEREGNQLTLLSAHLSDPSGLGRIVRDEAGAFLRIVEQKDASDAERAIDEVNGGIYVFDATALRQALGTIDRANAQGEMYLTDAAVRIQATGGRIQAVPAPDEWAIWGINDRVQLAAAAHVLNDRIIRRWQREGVTIVDPASTWIDVDVTLAEDVTILPGTQLHGATAIAAGATIGPDTTLVDTEVGEDAVVKRTDATLSVIGARASIGPWAYLRPNSVVGEDGKIGTFVETKNTQLGAGSKVPHLSYIGDATIGEGSNIGAGTITANYDGVEKHRTTVGSHVRTGSDNVFVAPVTIGDGAYTGAGTIVRKDVEPGALAISVAPQRTMSGWVESNRPGSKAADAAAAAGTQSPNA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ASHR01000014
EMBL· GenBank· DDBJ
ERG64946.1
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.
FeedbackHelp