A0A949LAE9 · A0A949LAE9_9GAMM

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

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 site8-11UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site22UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site73UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site78-79UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site100-102UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site102Mg2+ (UniProtKB | ChEBI)
Binding site136UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site151UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site166UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site224Mg2+ (UniProtKB | ChEBI)
Binding site224UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site330UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site348UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site360Proton acceptor
Binding site363UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site374UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site377acetyl-CoA (UniProtKB | ChEBI)
Binding site383-384acetyl-CoA (UniProtKB | ChEBI)
Binding site402acetyl-CoA (UniProtKB | ChEBI)
Binding site420acetyl-CoA (UniProtKB | ChEBI)
Binding site437acetyl-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
      KUG83_01650

Organism names

Accessions

  • Primary accession
    A0A949LAE9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-226Pyrophosphorylase
Domain5-119MobA-like NTP transferase
Region227-247Linker
Region248-453N-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
    453
  • Mass (Da)
    48,592
  • Last updated
    2023-02-22 v1
  • Checksum
    30DE0C5CF0098FE0
MALEVIILAAGKGTRMKSVKPKVLHELAGKSLVARVVEIAKSLNPSKVHLVYGHGGEQIIAAFDGQPLNLIEQAEQKGTGHAVAQVLPDIDPDNEILILYGDVPLIDSETLNRLTEKASSGFSLLTVDLPSPDGYGRIVRDTDEKVVAIVEHKDASFAQLAITEVNTGVMCVSGACLRRWLPLLSSENSQGEYYLTDIVAMAESEDICIETEQPKETFEVEGINDRLQLSRMERVFQIKQAEKLMAQGVTLMDPARFDLRGTLSAGTDSTIDINVVIEGEVTLGSNIRIGPNCVIRNSSIGDGVEILANSLIEDSKVSNDCIIGPYARLRPGSELKSNVKVGNFVEIKKSTLEVGSKVNHLSYIGDATVGEHANIGAGTITCNYDGVNKFQTEIGAGAFIGSNTSLIAPVKIGKNATTGAGSAISKDVSDENLAIARGKQRNIDTWQRPVKKT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAHRVS010000067
EMBL· GenBank· DDBJ
MBV1871228.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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