A0A0H2UUC4 · A0A0H2UUC4_STRP3

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.

Type
IDPosition(s)Description
Active site108Nucleophile
Binding site143substrate
Active site207

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
    • Ordered locus names
      SpyM3_0667

Organism names

Accessions

  • Primary accession
    A0A0H2UUC4

Proteomes

Interaction

Subunit

Forms a heterodimer with MurT.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain19-214CobB/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
    263
  • Mass (Da)
    29,573
  • Last updated
    2015-09-16 v1
  • MD5 Checksum
    C46191247E79BF47A7E976C3B4796A01
MTYTSLKSPENQDYIYDLNIAHLYGNLMNTYGDNGNILMLKYVAEKLGARVTVDIVSINDTFEQDDYDIVFFGGGQDYEQSIVAKDLPSKKAALADYIANNKVVLAICGGFQLLGQYYVQANGVKIDGLGIMGHYTLNQHQNRFIGDIKIHNDEFNETYYGFENHQGRTFLSGDEKPLGQVVYGNGNNKEDQTEGVHYKNVYGSYFHGPILSRNVNLAYRLVTTALKKKYGSAISLPSYDDILKQEITEEYADLKSKASFNKV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014074
EMBL· GenBank· DDBJ
AAM79274.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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