S9SB63 · S9SB63_9RHOB

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 site11-14UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site25UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site78UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site83-84UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site106-108UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site108Mg2+ (UniProtKB | ChEBI)
Binding site144UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site159UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site174UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site231Mg2+ (UniProtKB | ChEBI)
Binding site231UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site320UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site338UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Active site350Proton acceptor
Binding site353UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site364UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site367acetyl-CoA (UniProtKB | ChEBI)
Binding site373-374acetyl-CoA (UniProtKB | ChEBI)
Binding site392acetyl-CoA (UniProtKB | ChEBI)
Binding site410acetyl-CoA (UniProtKB | ChEBI)
Binding site427acetyl-CoA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functioncarbohydrate derivative binding
Molecular Functionglucosamine-1-phosphate N-acetyltransferase activity
Molecular Functionglutamine-fructose-6-phosphate transaminase (isomerizing) activity
Molecular Functionmagnesium ion binding
Molecular FunctionUDP-N-acetylglucosamine diphosphorylase activity
Biological Processcell morphogenesis
Biological Processcell wall organization
Biological Processfructose 6-phosphate metabolic process
Biological Processglutamine metabolic process
Biological Processlipid A biosynthetic process
Biological Processpeptidoglycan biosynthetic process
Biological Processprotein N-linked glycosylation
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
      ruthe_00769

Organism names

Accessions

  • Primary accession
    S9SB63

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homotrimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-233Pyrophosphorylase
Region234-254Linker
Region255-1087N-acetyltransferase
Region449-478Disordered
Compositional bias457-475Polar residues
Domain485-700Glutamine amidotransferase type-2
Domain949-1077SIS

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
    1,087
  • Mass (Da)
    116,697
  • Last updated
    2013-10-16 v1
  • Checksum
    9C8C4830DE4338D9
MEGTGIAVVILAAGAGTRMESDRPKVLHELGGAPLLHHAMRTAAAIGPERVVVVTGVGAEAVEAAARAFDPDAVCVRQAEQLGTAHAVQQAAAALADHGGDVLVLYGDTPFVRPETIEAMQQARARADIVVLGFETADPQARYGRLVTDEGDGLLGIVEWKDADAATRAIRLCNSGVLLAEGAFLFALLREVDRANAAGEYYLTDVVALARGRGLRATVVRCEEAETLGVNSRAELRAAEAALQARMRAQALEDGVSMPLPETVVFAYDTVVGRDAVIESHVVFGPGVTVESGARIRAFSHLEGCHVSRGAIVGPFARLRPGAELAEAVHVGNFVEVKAAVLHEGVKVNHLSYVGDAEVGERTNIGAGTITCNYDGVSKHRTVIGREAFIGSDTMLVAPVRLGDGAVTASGSVITEDVPAGALALGRARQVVKPGLGARLMERLRAAKAARTKAPPGTGTGTGTGTGTGTGTGTGNDDGRGGLMCGIVGILGRHEVAPLLVEALRRLEYRGYDSAGVATVHEGRLDRRRAVGKLVNLSDLLVHAPLPGRSGIGHTRWATHGGPVEANAHPHRAGRVCVVHNGIIENFRELRAWAATQGLATESETDSEMVAVLCDHFLARGASPAEAVDRTLERVTGAYALAFLFEGEEDLLIVARKGSPLAIGHGEGEMFVGSDALALAPLTDRITYLEDGDRAVITRAGAEIRDAAGRPVSRPIRRIALDAVQVDKAGHRHFMAKEIAEQPGRLQDVLSHYLGEGGVRLPEGLDFRDYDRVTMVACGTAAYACQVARYWFEQVARLPAEVDVASEFRYRERPCHRGRWRCSSASRARRPTRWQRCATAGGGRRGRWRWSMWPNPPSPGRRTWCCRSWQGGRSASPRPRPLPVSLRFWGFWRCGRPRIAGRCPPPPMRRRWRRCRCCRASSTGRWTSRGRRGASPPIWPRRATSCSWGRGRMYPLALEGALKLKEISYIHAEGHASGELKHGPIALVDPLVPVIVLAPRDELFEKSVSNMQEVMARGGRVLLVTDRAGAQEAGEGVWETLVMPEIAPLWAPILYAVPAQLLAYHTAVAKGTDVDQPRNLAKSVTVE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias457-475Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AOLV01000008
EMBL· GenBank· DDBJ
EPX87370.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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