W9T7Y4 · W9T7Y4_9PSED

  • Protein
    Bifunctional protein GlmU
  • Gene
    glmU
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

TypeIDPosition(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 site99-101UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site101Mg2+ (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

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
      BAY1663_00938

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BAY1663
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    W9T7Y4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-226Pyrophosphorylase
Domain6-126MobA-like NTP transferase
Region227-247Linker
Region248-454N-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
    454
  • Mass (Da)
    48,217
  • Last updated
    2014-05-14 v1
  • Checksum
    1DC2602588DE1E10
MSLDIVILAAGQGTRMRSSLPKVLHPVAGKSMLGHVIDTARALQPRSIQVVIGHGAEQVRQCLAGEDLNYVVQAEQLGTGHAVAQALPNLAAERVLILYGDVPLIEAETLQRLLHKVGPEQLALLTVVLDDPSGYGRIVRDAQGEVQAIIEHKDASAEQRAIREGNTGILAVPGSRIGEWLGRLSNSNVQGEYYLTDVIAMAVADGLRVATEQPLDAMEVQGANDRIQLAELERHYQRRAARRLMAEGVTLRDPARFDLRGDVSVGRDVLIDVNVILEGSVIIEDGVSIGPNCVIRDSTLRKGAIVKANSHLEGAELGEGADCGPFARLRPGSVLGARAHVGNFVELKNATLAEGAKAGHLSYLGDAEIGARSNIGAGTITCNYDGANKFRTVMGEDVFIGSNSSLVAPLNLGDGATTGAGSVITEDVPTHTLALGRGRQRNIDGWQRPSKQKP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AZSV01000008
EMBL· GenBank· DDBJ
EXF46578.1
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