Q3Y1G9 · Q3Y1G9_ENTFD

Function

function

The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The GatD subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia. The resulting ammonia molecule is channeled to the active site of MurT.

Catalytic activity

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site96Nucleophile
Binding site131substrate
Active site195

GO annotations

AspectTerm
Molecular Functioncarbon-nitrogen ligase activity on lipid II
Molecular Functionglutaminase activity
Biological Processcell wall organization
Biological Processcobalamin biosynthetic process
Biological Processglutamine metabolic process
Biological Processpeptidoglycan biosynthetic process
Biological Processregulation of cell shape

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit GatD
  • EC number
  • Alternative names
    • Lipid II isoglutaminyl synthase glutaminase subunit
      (EC:3.5.1.2
      ) . EC:3.5.1.2 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      cobQ
    • Synonyms
      gatD
    • ORF names
      HMPREF0351_12306

Organism names

Accessions

  • Primary accession
    Q3Y1G9

Proteomes

Interaction

Subunit

Forms a heterodimer with MurT.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-202CobB/CobQ-like glutamine amidotransferase

Sequence similarities

Belongs to the CobB/CobQ family. GatD subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    232
  • Mass (Da)
    26,164
  • Last updated
    2005-10-11 v1
  • Checksum
    57E47950876601C7
MANYELNIAHLYGNLMNTYGDNGNLLMLKYIAEKMGVSCHTEIVSIHEPFDADKYDLVFFGGGQDFEQLIISKDIQKKKDSLINYIENDGVMLAICGGYQLLGHYYMGANGEKIQGISALDHYTLSQENNRFIGDIVIHNEEFNETYYGFENHNGRTFLGEGERPLGKVVQGQGNNGEDQSEGVIYRNVFGSYFHGPILARNENLAARLIRLALEQRYGKELDLPYLEGQTA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP003583
EMBL· GenBank· DDBJ
AFK59930.1
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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