A0A0E1XAT9 · A0A0E1XAT9_STAAU

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site94Nucleophile
Binding site128substrate
Active site189

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
      gatD
    • ORF names
      HMPREF0769_11281

Organism names

Accessions

  • Primary accession
    A0A0E1XAT9

Proteomes

Interaction

Subunit

Forms a heterodimer with MurT.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain5-196CobB/CobQ-like glutamine amidotransferase
Region219-243Disordered

Sequence similarities

Belongs to the CobB/CobQ family. GatD subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    243
  • Mass (Da)
    27,444
  • Last updated
    2015-05-27 v1
  • Checksum
    D37566871EFCA326
MHELTIYHFMSDKLNLYSDIGNIIALRQRAKKRNIKVNVVEINETEGITFDECDIFFIGGGSDREQALATKELSKIKTPLKEAIEDGMPGLTICGGYQFLGKKYITPDGTELEGLGILDFYTESKTNRLTGDIVIESDTFGTIVGFENHGGRTYHNFGTLGHVTFGYGNNDEDKKEGIHYKNLLGTYLHGPILPKNYEITDYLLEKACERKGIPFEPKEIDNEAEKQAKQVLIDRANRQKKSR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ACJA02000002
EMBL· GenBank· DDBJ
EFH95898.1
EMBL· GenBank· DDBJ
Genomic DNA

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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