A0A1S6WU89 · A0A1S6WU89_9HYPH

  • Protein
    Bifunctional protein GlmU
  • Gene
    glmU
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

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.

Type
IDPosition(s)Description
Binding site10-13UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site24UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site77UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site82-83UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site107Mg2+ (UniProtKB | ChEBI)
Binding site143UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site157UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site172UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site229Mg2+ (UniProtKB | ChEBI)
Binding site229UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site318UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site336UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site348Proton acceptor
Binding site351UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site362UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site365acetyl-CoA (UniProtKB | ChEBI)
Binding site371-372acetyl-CoA (UniProtKB | ChEBI)
Binding site390acetyl-CoA (UniProtKB | ChEBI)
Binding site408acetyl-CoA (UniProtKB | ChEBI)
Binding site425acetyl-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
      BWD162_007550

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • WD16.2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Bartonellaceae > Bartonella

Accessions

  • Primary accession
    A0A1S6WU89

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-231Pyrophosphorylase
Domain8-132MobA-like NTP transferase
Region232-252Linker
Region253-449N-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
    449
  • Mass (Da)
    48,702
  • Last updated
    2017-05-10 v1
  • Checksum
    9C8686363CC2E996
MIRSCLSIVLAAGEGTRMKSFLPKVLHKVAGLPLICHVVKQVELAGFSQLAVVVGAGGEDVIKVVQSCVKNVMIFEQKERLGTAHAVLSARLALQKGIDDVLIIFGDTPLIEHASLTRIRAPLAMGADVVIAGFYAPDPTGYGRLIKKDGKFIAIVEEKDASDEEKKNSFCNGGIMAINGKHALSLLDKINNDNAQQEYYLTDIVSIASREGLDVRAIEVPFDNVIGVNNCFELSEVDTLWQKRKARDFMLSGVTILKPESVYFSYDTEIEPGVLIEPNVYFGPGVKIQSGAVIRAFSYLEGAFVGADTQIGPYARLRPGTELARSVKIGNFCEIKQAKVGEAAKVNHLSYIGDAEIGSHTNIGAGTITCNYDGFHKYKTMIDDNVFIGSNSALIAPLIIGKNSYIASGSVITEDVPINSLAFGRARQVIKENRATKLRTHLSIDKQKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP019781
EMBL· GenBank· DDBJ
AQX19872.1
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