A0A7W7D5T5 · A0A7W7D5T5_9ACTN

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

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site12-15UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site26UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site79UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site84-85UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site107-109UDP-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 site234Mg2+ (UniProtKB | ChEBI)
Binding site234UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site339UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site357UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site369Proton acceptor
Binding site372UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site383UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site386acetyl-CoA (UniProtKB | ChEBI)
Binding site392-393acetyl-CoA (UniProtKB | ChEBI)
Binding site411acetyl-CoA (UniProtKB | ChEBI)
Binding site429acetyl-CoA (UniProtKB | ChEBI)
Binding site446acetyl-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
      BJ982_002266

Organism names

  • Taxonomic identifier
  • Strain
    • DSM 45784
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Streptosporangiales > Streptosporangiaceae > Sphaerisporangium

Accessions

  • Primary accession
    A0A7W7D5T5

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-236Pyrophosphorylase
Domain9-147MobA-like NTP transferase
Region237-257Linker
Region258-503N-acetyltransferase
Region460-503Disordered

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    503
  • Mass (Da)
    52,213
  • Last updated
    2021-06-02 v1
  • Checksum
    624248B4C2215A5D
MSVPRPAAVIVLAAGEGTRMKSSTPKVLHELCGRPLVDHVLASARGLSPERLIVVIGHAREQVEAHLTAAGPDTRAVVQAEQKGTGHAVRTVLESVGTIGGTVLVTYGDTPLLRTETLAGLLSSHAADGNAVTVLTAEVPDPTGYGRIIRDDSGAVLQIVEERDATPRQRAVKEMNSGVYAFDGSLLADAVKRVSTANAQGEEYLTDVLSILREDGHRVGAHIAPDHVEVEGVNDRAQLAFARAVLNSRILRAHMRAGVTVIDPATTWVDVGVTLEPDVVIHPGTQLHGRTSVASGAEVGPATTLTDTAVGAGAVVRNSVCDGAEIGPGASVGPYAYLRPGTVLGRRAKAGTYVEMKNARLGDGSKVPHLTYVGDATIGEGSNIGASSVFVNYDGVRKHHTTVGDHVRVGSDNMLVAPVTIGDGAYTAAGSVITNDVPPGAMAVGRARQRTIEGWVARRRAGTASDEAARRALEGRGAVSADGRQTSAGDQGPSGEQHRENSK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACHND010000001
EMBL· GenBank· DDBJ
MBB4700722.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
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