A0A6I1EGE3 · A0A6I1EGE3_9BURK

  • 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.
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.

Type
IDPosition(s)Description
Binding site6-9UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site20UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site72UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site77-78UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site102Mg2+ (UniProtKB | ChEBI)
Binding site137UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site152UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site167UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site225Mg2+ (UniProtKB | ChEBI)
Binding site225UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site331UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site349UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site361Proton acceptor
Binding site364UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site375UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site378acetyl-CoA (UniProtKB | ChEBI)
Binding site384-385acetyl-CoA (UniProtKB | ChEBI)
Binding site403acetyl-CoA (UniProtKB | ChEBI)
Binding site421acetyl-CoA (UniProtKB | ChEBI)
Binding site438acetyl-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
      GBM95_11050

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ASD393
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Sutterellaceae > Sutterella

Accessions

  • Primary accession
    A0A6I1EGE3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-227Pyrophosphorylase
Domain4-127MobA-like NTP transferase
Region228-248Linker
Region249-453N-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
    453
  • Mass (Da)
    48,614
  • Last updated
    2020-08-12 v1
  • Checksum
    7CBD592E0E296423
MNIVILAAGMGKRMHSRLPKVLQPIAGRPMIDHVLDATEGLSASPRVVVVGHGAENVMEHLADRSDVAFALQSPQLGTGHALRQALGQLDRNESKTLVCLGDVPLLSRETLAAIASEAEKSDLVLLTVELDNPTGYGRILRNTMGFVRAIVEEKDASPEERLVREVNTGIMCLPTSRLDGWLSSLKAANAQGEYYLTDVIGLAADEGLRITTVHPGHVWEVEGVNSKAQLASLERVWQKEQARRLLDAGVTLIDPARIDIRGILECGKDVEIDVNCVFEGHVRIADGVRIGANCVIRDAEIGEDTEILPFCHIEGARIGMNGRIGPYSRLRPGAELIGGNHIGNFVEVKKSMVGIGTKINHLTYIGDADIGAHVNIGAGTITCNYDGVNKFRTRIGDDAFIGSGTELVAPVEVGAGATIGAGSTITKKVPEGKLTVARSRQVTIEGWHRPVKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WEHX01000131
EMBL· GenBank· DDBJ
KAB7653142.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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