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J2ZAA2 · J2ZAA2_9PSED

  • 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 site7UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site58UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site63-64UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site84-86UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site86Mg2+ (UniProtKB | ChEBI)
Binding site121UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site136UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site151UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site209Mg2+ (UniProtKB | ChEBI)
Binding site209UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site315UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site333UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site345Proton acceptor
Binding site348UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site359UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site362acetyl-CoA (UniProtKB | ChEBI)
Binding site368-369acetyl-CoA (UniProtKB | ChEBI)
Binding site387acetyl-CoA (UniProtKB | ChEBI)
Binding site405acetyl-CoA (UniProtKB | ChEBI)
Binding site422acetyl-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
      PMI26_00132

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • GM33
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    J2ZAA2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-211Pyrophosphorylase
Domain6-108MobA-like NTP transferase
Region212-232Linker
Region233-440N-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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    440
  • Mass (Da)
    47,319
  • Last updated
    2012-10-03 v1
  • MD5 Checksum
    044297437334629520917ECA2F327417
MRSALPKVLHPIAGNSMLGHVIHSARQLDPQRIHVVIGHGADAVRERLAADDLNFVLQDKQLGTGHAVAQAVPFIQSDNVLVLYGDVPLIEVDTLQRLLKQVGPEQLALLTVELDDPTGYGRIVRDAQGKVTAIVEQKDTNEAERKITEGNTGILALPFARLGDWMSRLSNNNAQGEYYLTDIIAMAVSDGLVVATEQPHDAMEVQGANDRKQLSELERHYQLRAGRRLMAQGVTLRDPARFDIRGDVTVGRDVLIDINVILEGKVVIEDDVVIGPNCVIKDSTLRKGVVIKANSHIEGAILGEGSDAGPFARLRPGTVLEARAHVGNFVELKNAHLGEGAKAGHLTYLGDAEVGARTNIGAGTITCNYDGANKWKTVLGEDVFIGSNNSLVAPVDILDGATTAAGSTITSTVDKSQLAIGRARQKNIDGWKRPEKVKKG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AKJO01000003
EMBL· GenBank· DDBJ
EJM49918.1
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.
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