A0A381M438 · A0A381M438_XANCJ

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 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

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
      XSP_000594
      , XSP_000595

Organism names

Accessions

  • Primary accession
    A0A381M438

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-228Pyrophosphorylase
Domain7-137MobA-like NTP transferase
Region229-249Linker
Region250-454N-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
    454
  • Mass (Da)
    47,847
  • Last updated
    2018-11-07 v1
  • Checksum
    BB23C217E61A6767
MTLPLHVVILAAGEGKRMRSSLPKVLQPLAGQPMLAHVIATARQLQPAAIHVVHGHGGEQVQAAFAAQGDLHWAEQRQQLGTGHAVQQAMDAIPDAATVLVLYGDVPLIQPQDLLQLLHAPGRMAVLVADVPNPTGYGRILRDAEGKVAAIVEQKDANDEQRRIRTINTGILTAESTALRRWLAGLSNENAQGEFYLTDVFASAAADFTPADMVHVADAQDVEGANDPWQLAQLERAWQLRAARALCLQGVRMADPARVEQRGTVTVGSDVQLDIDVILEGDVTLGDGVVVGPFVRLRDVTLGAGTQVRAHCDLEGVVTEGAVQIGPFARLRPGTVLADGVHIGNFVETKKVTMGVGSKANHLTYLGDAVIGSKVNIGAGTITCNYDGVNKSQTSIGDGAFVGSNSALVAPIEIGAMATIGAGSVITRDAPAGQLSVTRARQTVVEGWERPTKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LR824643
EMBL· GenBank· DDBJ
CAD0313781.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861807
EMBL· GenBank· DDBJ
CAD1787455.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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