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A0AAN3XDH1 · A0AAN3XDH1_LACRH

Function

function

The lipid II isoglutaminyl synthase complex catalyzes the formation of alpha-D-isoglutamine in the cell wall lipid II stem peptide. The MurT subunit catalyzes the ATP-dependent amidation of D-glutamate residue of lipid II, converting it to an isoglutamine residue.

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 binding site, active site.

Type
IDPosition(s)Description
Binding site208Zn2+ (UniProtKB | ChEBI)
Binding site211Zn2+ (UniProtKB | ChEBI)
Binding site230Zn2+ (UniProtKB | ChEBI)
Binding site233Zn2+ (UniProtKB | ChEBI)
Active site358

GO annotations

AspectTerm
Molecular Functionligase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT
  • EC number

Gene names

    • Name
      murT
    • ORF names
      LRHMDP2_1678

Organism names

Accessions

  • Primary accession
    A0AAN3XDH1

Proteomes

Interaction

Subunit

Forms a heterodimer with GatD.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain56-189Mur ligase central
Domain322-433Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT C-terminal

Sequence similarities

Belongs to the MurCDEF family. MurT subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    450
  • Mass (Da)
    49,409
  • Last updated
    2024-10-02 v1
  • MD5 Checksum
    156FA0E0CE22B293221725CB16E57B89
MAFSAKASLATAIGRSSYWFLHTFFKGGSSLPGKLANRLDPHVLQALGHNYDVIVVTGTNGKTLTTSLIVKVLKQKYQEVLTNPTGSNMLQGITTAFLAQPKSGHGRGIAVLEVDEANVAPVAAQLKPKAFVLTNIFRDQMDRYGEFYTTYQKILDGITLDPTAVVLANGDAPIFSSRKLPNPIYYYGFTLTNEGDHKAPPNTDGVLCPVCQHILHYHALTYANLGNFFCPNCGFKRPELTYQVNAVTKMTPQSSEFAIDGQPCHIDIGGMYNIYNALAAFAVGRTFDVSPEQISQAFAYDEKVFGRQEVIQLGTKKLTLILVKNPVGLNQVLSMIQTAKQPFGFAMLLNANYADGIDTSWIWDGNFEEFVASKKAADYLVGGERYQDIALRLKVAGVPETKLTIKPDLGDVLTTLQEMPQQQLYVLATYTAMLQLRKKLSDGGYIKGGF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AMQW01000007
EMBL· GenBank· DDBJ
EKS51273.1
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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