A0A3S4KW49 · A0A3S4KW49_AVIVO

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

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 site74UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site79-80UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site101-103UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site103Mg2+ (UniProtKB | ChEBI)
Binding site138UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site152UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site167UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site225Mg2+ (UniProtKB | ChEBI)
Binding site225UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site331UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site349UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site361Proton acceptor
Binding site364UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site375UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site378acetyl-CoA (UniProtKB | ChEBI)
Binding site384-385acetyl-CoA (UniProtKB | ChEBI)
Binding site403acetyl-CoA (UniProtKB | ChEBI)
Binding site421acetyl-CoA (UniProtKB | ChEBI)
Binding site438acetyl-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
      NCTC3438_00420

Organism names

Accessions

  • Primary accession
    A0A3S4KW49

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-227Pyrophosphorylase
Domain6-126MobA-like NTP transferase
Region228-248Linker
Region249-456N-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
    456
  • Mass (Da)
    49,532
  • Last updated
    2019-04-10 v1
  • Checksum
    4BCBD0F71BBCD704
MKNLSVVILAAGKGTRMYSDLPKVLHKVAGKPMVKHVIDTAKQLNADNIHLIYGHGAELLQQHLADENVNWVLQPVQLGTGHAMQQAAPFFADDENIVMLYGDAPLITAQTLQKLIDAKPENGIALLTAHLDDPTGYGRIIRQDGNVVAIVEQKDATPEQLAIQEVNTGVMVSSGASFRKWLAKLDNNNAQGEYYMTDVIKFANQDGCKVAAVQAQDLMEVEGANNRLQLAELERYYQRKQAEKLLLAGVSLRDPSRFDLRGEILHGKDVEIDVNVIIEGNVKLGDRVKIGAGCIIKDCVIGDDVEIKPYSVFEDAVIGEQAQIGPFSRLRPGTELAAQTHIGNFVEVKKSHIGKGSKVNHLSYVGDSEIGANCNIGAGTITCNYDGVNKFKTVIGDDVFVGSDSQLVAPVTIAKGATIGAGTTVTKDIAENELVISRVPQRNIQGWKRPEKLEKK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LR134167
EMBL· GenBank· DDBJ
VEB22381.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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