Q8PGH2 · GLMU_XANAC

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 site10-13UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site24UDP-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 site103-105UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site105Mg2+ (UniProtKB | ChEBI)
Binding site138UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site153UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site168UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site226Mg2+ (UniProtKB | ChEBI)
Binding site226UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site332UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site350UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site362Proton acceptor
Binding site365UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site376UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site379acetyl-CoA (UniProtKB | ChEBI)
Binding site385-386acetyl-CoA (UniProtKB | ChEBI)
Binding site404acetyl-CoA (UniProtKB | ChEBI)
Binding site422acetyl-CoA (UniProtKB | ChEBI)
Binding site439acetyl-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
      XAC3644

Organism names

Accessions

  • Primary accession
    Q8PGH2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002338811-456Bifunctional protein GlmU

Interaction

Subunit

Homotrimer.

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-228Pyrophosphorylase
Region229-249Linker
Region250-456N-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
    456
  • Mass (Da)
    48,246
  • Last updated
    2006-05-02 v2
  • Checksum
    C9D1D78CDFC10B41
MTLPLHVLILAAGEGKRMRSSLPKVLQPLAGQPMLAHVIATARQLQPAAIHIVYGHGGDQVQAAFADQGDLQWAEQREQLGTGHAVQQAMPAIPDAATVLVLYGDVPLIRSESLLQLLHAPGRMAVLVAELANPTGYGRILRDAEGKVAAIVEQKDANDEQRRIRTINTGILTAESTALRRWLAGLSNDNAQAEFYLTDVFASAAADFTPADMVHVADPQDVEGANDPWQLAQLERAWQLRAARTLCLQGVRMADPARVEQRGSVQVGRDVQLDIDVILEGNVTLGDDVVIGPFVRLRDVTLGAGTQVRAHSDLEGVITEGAVQIGPFARLRPGTVLADGVHIGNFVETKKVTMGVGSKANHLTYLGDAVIGSKVNIGAGTITCNYDGVNKSQTTIGDGAFIGSNSALVAPIQIGANSTIGAGSVITSDAPAGQLSVTRARQTVVEGWKRPTKKSP

Sequence caution

The sequence AAM38487.1 differs from that shown. Reason: Erroneous initiation

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE008923
EMBL· GenBank· DDBJ
AAM38487.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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