E3D7E5 · E3D7E5_GARV3

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 site113Nucleophile
Binding site147substrate
Active site211

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
    • Ordered locus names
      HMPREF0421_20090

Organism names

Accessions

  • Primary accession
    E3D7E5

Proteomes

Interaction

Subunit

Forms a heterodimer with MurT.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain25-218CobB/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
    268
  • Mass (Da)
    29,787
  • Last updated
    2011-01-11 v1
  • Checksum
    2D6DB323DDF64C6C
MNDMSDVNYISQANATNKAENRVLDIVSLYPKDMNIYGDYGNVLTIMRRAELYGYKPVLHEYNVGDDWPKRVDMVLGGGGQDHGQSRVTDDLFARAGAIRELAKNGVPMLMICGLYQLFGEYFETIEGQKLKGIGILGEHTVGQDVRMIGNLVEHSRDFGDIVGYENHSGRTSLESGTQPLGSVDGENCGNNGEDHTEGARKYNVIGTYMHGSVLPKNPRLSDFLIRTAAQNRYGEFAPKQTNAQRAELEKLDELANRAREVAITRPR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002104
EMBL· GenBank· DDBJ
ADP38176.1
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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