A1A1R9 · GLMU_BIFAA

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

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.
Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.

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 site76UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site81-82UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site109Mg2+ (UniProtKB | ChEBI)
Binding site146UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site161UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site176UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site233Mg2+ (UniProtKB | ChEBI)
Binding site233UDP-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 site391-392acetyl-CoA (UniProtKB | ChEBI)
Binding site428acetyl-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

    • UPA00113UER00532
    • UPA00113UER00533
    • UPA00973

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
    • Ordered locus names
      BAD_0871

Organism names

Accessions

  • Primary accession
    A1A1R9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000561391-460Bifunctional protein GlmU

Proteomic databases

Interaction

Subunit

Homotrimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-235Pyrophosphorylase
Region236-256Linker
Region257-460N-acetyltransferase

Sequence similarities

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.
In the C-terminal section; belongs to the transferase hexapeptide repeat family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    460
  • Mass (Da)
    48,981
  • Last updated
    2007-01-23 v1
  • Checksum
    E243BA4B85253779
MALSAAIILAAGEGTRMRSNKPKVLHTLAGKTFLNRVMDSVAALDPDTLAVVVHYQAERVAEAARSYNEHVTIVEQDDIPGTGRAVQCAMAQLTQKDDLDGAVLIAASDMPLLDTDTLDQLLAFHEKSGNGATVLTTILDDPTGYGRIIRDSEGNVLRIVEQKDANSSELAVREVNTSVYVFDAKLLAEAIANLKSNNAQGEFYLTDALEAAKANGAVGAFAAPDPLSVEGVNDRVQLAALAKAHNKRVCEHWMREGVTILDPDTTWIEDDVQIARDAVILPGCFLQGHTVIGEAAEVGPYTTLIGATIDAEAHVERSRVQETHIGRAANIGPWTYLRPGNELGEGSKAGAFVEMKKAHIGNGTKVPHLSYVGDADLGEHTNIGGGTITANYDGVHKHHTTIGSNVHVGAGNLFVAPVTVGDGVTTGAGSVVRHDVPSDSMVYSENTQHVVEGWKPEWER

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP009256
EMBL· GenBank· DDBJ
BAF39652.1
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