F0GZJ6 · F0GZJ6_9FIRM

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.
Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).

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

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 Mg2+ ions per subunit.

Pathway

Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1.
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 site7-10UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site21UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site78-79UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site102Mg2+ (UniProtKB | ChEBI)
Binding site139UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site153UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site168UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site226Mg2+ (UniProtKB | ChEBI)
Binding site226UDP-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 site384-385acetyl-CoA (UniProtKB | ChEBI)
Binding site403acetyl-CoA (UniProtKB | ChEBI)
Binding site421acetyl-CoA (UniProtKB | ChEBI)
Binding site438acetyl-CoA (UniProtKB | ChEBI)
Binding site512-514ATP (UniProtKB | ChEBI)
Binding site571-572ATP (UniProtKB | ChEBI)
Binding site605Mg2+ (UniProtKB | ChEBI)
Binding site646Mg2+ (UniProtKB | ChEBI)
Active site669
Binding site671D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site695D-ribose 5-phosphate (UniProtKB | ChEBI)
Binding site699-703D-ribose 5-phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentribose phosphate diphosphokinase complex
Molecular FunctionATP binding
Molecular Functionglucosamine-1-phosphate N-acetyltransferase activity
Molecular Functionkinase activity
Molecular Functionmagnesium ion binding
Molecular Functionribose phosphate diphosphokinase activity
Molecular FunctionUDP-N-acetylglucosamine diphosphorylase activity
Biological Process5-phosphoribose 1-diphosphate biosynthetic process
Biological Processcell morphogenesis
Biological Processcell wall organization
Biological Processlipid A biosynthetic process
Biological Processpeptidoglycan biosynthetic process
Biological Processphosphorylation
Biological Processpurine nucleotide biosynthetic process
Biological Processregulation of cell shape
Biological Processribonucleoside monophosphate biosynthetic process
Biological ProcessUDP-N-acetylglucosamine biosynthetic process

Keywords

Enzyme and pathway databases

    • UPA00087UER00172
    • UPA00113UER00532
    • UPA00973

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
    • Synonyms
      prs
    • ORF names
      HMPREF9246_0678

Organism names

Accessions

  • Primary accession
    F0GZJ6

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer.
Homotrimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-228Pyrophosphorylase
Domain3-216Nucleotidyl transferase
Region229-249Linker
Region250-791N-acetyltransferase
Domain479-595Ribose-phosphate pyrophosphokinase N-terminal

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
    791
  • Mass (Da)
    87,390
  • Last updated
    2011-05-03 v1
  • MD5 Checksum
    FBE304E553CF217B210E492128FFFE04
MLKNIILAAGEGTRMKSNTSKVMTKILNRELITYIVDACSFENSKTIIIGGKNKSLLEEKYPNLEIKEQKIGDDFPYGTAYAVSMAIDLIDENDDCLILNGDIPLITKKSLEDFINFHKENNNNLTVMSTKIDNPTGYGRIIRKDNKFQKIVEEKDASIDEKKVNEINVGIYAFKGKDLKESLKKIDTNNNSNEYYLTDCIEILNNEGKKVESFVADNPDQFYGINNKKELANAAKLLRERINDYHMLNGVIIENPSIVNIEKGVKIGKDTIISGPCKILGDTEIGENCFIEGSSRIEDSIIKDNVKIDNSVIEKSFVGQGTDIGPFSHLRPKAKLGKNVHIGNFVEVKNANVDDGTKAGHLAYIGDCDLGKDINIGCGVIFVNYDGKFKHRSKIEDGAFIGSNSNIVAPVHVKKEGYIAAGSTITKDVDEGVLSIERAEQKNIPGYVEKRKKRFRKIKGAKIKMSESTSSAHINRGEMILFAGNSNPELAKAVAKSLGLELGKVEVKKFADSEINIKINEAVRGKDVYIIQPTSYPTNDNLMELLIMTDACRRASAKYVNVVVPYYGYARQDRKTRGREPISAKLVANLITVSGADRVITMDLHAGQIQGYFDIPVDHFSAVKLLSSHFKEAYNNPDEYVVVSPDLGGVTRARKFADSLKLTIAIIEKRRPRPNVSEVMNVIGDFEGKHCILVDDMIDTAGTICNAANYLKDHGAKDVSIAATHGVLSGDACKKLENACVKEVVITDTIKIPENKKIGKIKQMSIAPLLAEAIHRINTNESISGLFDDEI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AEXN01000011
EMBL· GenBank· DDBJ
EGC84507.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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