A4VWR1 · GLMU_STRSY

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 site73UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site78-79UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site103Mg2+ (UniProtKB | ChEBI)
Binding site140UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site155UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site170UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site228Mg2+ (UniProtKB | ChEBI)
Binding site228UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site333UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site351UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site363Proton acceptor
Binding site366UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site377UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site380acetyl-CoA (UniProtKB | ChEBI)
Binding site386-387acetyl-CoA (UniProtKB | ChEBI)
Binding site405acetyl-CoA (UniProtKB | ChEBI)
Binding site423acetyl-CoA (UniProtKB | ChEBI)
Binding site440acetyl-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
      SSU05_1584

Organism names

Accessions

  • Primary accession
    A4VWR1

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003377421-460Bifunctional protein GlmU

Interaction

Subunit

Homotrimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-230Pyrophosphorylase
Region231-251Linker
Region252-460N-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)
    49,350
  • Last updated
    2008-05-20 v2
  • Checksum
    5F2BBC816D458F7F
MSNNYAIILAAGKGTRMKSDLPKVLHKVAGITMLEHVKRAVDAMEPAKTVTIVGHKAELVQAVLEGQSEFALQSEQLGTGHAVMMAEPALAGLEGQTLVIAGDTPLITGESLKNLINFHVSHKNVATILTAQADNPFGYGRIIRNADGEVQKIVEQKDANDFEKQVKEINTGTYLFDNKRLFEALKDINTDNAQGEYYLTDVISIFRQAGEKVGAYVLRDFDESLGVNDRVALATAEAVMRKRINEKHMVNGVTFINPDATYIDIDVEIGAEAVIEANVVLKGQTVIGERTVLTNGTRVRDAKIAADAVISNSDIEESVIEEGVTVGPYAHIRPGSLLKKDVHVGNFVEIKASTLGQGTKSGHLTYLGNATIGNNVNVGAGTITVNYDGKNKFKTTVGDNAFVGSNSTIIAPVTIGDNALLAAGSVITKDIPEDAIGIGRGRQENKEGYATRFPFHPSQK

Sequence caution

The sequence ABP90550.1 differs from that shown. Reason: Erroneous initiation

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000407
EMBL· GenBank· DDBJ
ABP90550.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

Similar Proteins

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