M9R7G8 · M9R7G8_9RHOB

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 site8-11UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site22UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site75UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site80-81UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site103-105UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site105Mg2+ (UniProtKB | ChEBI)
Binding site140UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site154UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site169UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site226Mg2+ (UniProtKB | ChEBI)
Binding site226UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site315UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site333UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site345Proton acceptor
Binding site348UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site359UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site362acetyl-CoA (UniProtKB | ChEBI)
Binding site368-369acetyl-CoA (UniProtKB | ChEBI)
Binding site387acetyl-CoA (UniProtKB | ChEBI)
Binding site405acetyl-CoA (UniProtKB | ChEBI)
Binding site422acetyl-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
      OAN307_c20810

Organism names

  • Taxonomic identifier
  • Strain
    • 307
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Octadecabacter

Accessions

  • Primary accession
    M9R7G8

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-228Pyrophosphorylase
Domain6-132MobA-like NTP transferase
Region229-249Linker
Region250-450N-acetyltransferase
Region429-450Disordered

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
    450
  • Mass (Da)
    47,496
  • Last updated
    2013-06-26 v1
  • Checksum
    583DF1361197E991
MTVALIILAAGKGTRMMSDIPKVLHEVAGGSLLVHAMMSGSNLEPERTVVVAGYGADAVGAVAQAFDEDAIVVIQQEQLGTGHAVLQARAALVDFDGDVIILYGDTPFIQPETLDAMLAARKASDVVVLGFKAADPGRYGRLVMTGDTLERIVEFKDSSNEERAISLCNSGVIAARSDVLFDLLDAVSNDNAAGEYYLTDIIGIARAKDLSATVVRCDEAETMGVNSRTELADAEAAFQGRARKDAMANGVSLRAPDTVYFSFDTYIGPDSMVEPNVVFAAGVTVENNATIRAFSHLEGCHVSRGSVVGPYARLRPGTELAENVKVGNFVEIKNAVIEAGAKVNHLSYIGDAHVGERSNIGAGTITCNYDGVSKHRTTIGADVFVGSNTMLVAPVTLGNESMTATGTIVTKNVPVGDMAVGRARQENKTGFARRMQQKFKSSAENAAKDS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP003740
EMBL· GenBank· DDBJ
AGI67713.1
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