H6SMD3 · H6SMD3_PARPM

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 site32-35UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site46UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site95UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site100-101UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site123-125UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site125Mg2+ (UniProtKB | ChEBI)
Binding site163UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site177UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site192UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site249Mg2+ (UniProtKB | ChEBI)
Binding site249UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site338UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site356UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site368Proton acceptor
Binding site371UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site382UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site385acetyl-CoA (UniProtKB | ChEBI)
Binding site391-392acetyl-CoA (UniProtKB | ChEBI)
Binding site410acetyl-CoA (UniProtKB | ChEBI)
Binding site428acetyl-CoA (UniProtKB | ChEBI)
Binding site445acetyl-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
      RSPPHO_00190

Organism names

Accessions

  • Primary accession
    H6SMD3

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-28
ChainPRO_500360712829-467Bifunctional protein GlmU

Interaction

Subunit

Homotrimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-251Pyrophosphorylase
Domain29-162MobA-like NTP transferase
Region252-272Linker
Region273-467N-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
    467
  • Mass (Da)
    48,886
  • Last updated
    2012-04-18 v1
  • Checksum
    7A902FC04D0C1816
MSRVQPCGTLGRVLFPLFRTLAPMSQTAAVVLAAGQGTRMRSSLPKVLHPLAGRPLVGHVLDALAPLAPARTVVVIGPGMEAVAQAVAPHPTVEQTERLGTAHAVLQARDALAGFTGTVLVLYGDTPLVPSATLERLVAAQTGPEAPAVVVLGFRPEDPTGYGRLLVGPEGLEGIVEEKDATSEQRALRLCNSGVMALEGRVAFELLAQVGNANAKGEYYLTDVVALARAAGRRCHVVESAAEDLLGVNSREDLATAERVVQERLRRAAMSAGVTLSAPETVFFSWDTRLGEDVTVGPFVTFGPGVTVASGVEIKGFCHLEACTVATGALIGPYARLRPGARIAENAHIGNFVEIKNATVETGAKVNHLTYIGDARIGSRANIGAGTITCNYDGFFKHHTDIGADAFIGSNSALVAPVSVGDGAMVGAGSTITSDVPAGALALTRAPQETRDGWARRFVERMRRLKR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HE663493
EMBL· GenBank· DDBJ
CCG06816.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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