A0A0E3YVK4 · A0A0E3YVK4_9BACT

Function

function

Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site75UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site156-162ATP (UniProtKB | ChEBI)
Binding site197-198UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site224UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site230UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site232UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site428meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site452-455meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site503meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site507meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular FunctionUDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity
Biological Processcell division
Biological Processcell wall organization
Biological Processpeptidoglycan biosynthetic process
Biological Processregulation of cell shape

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
  • EC number
  • Alternative names
    • Meso-A2pm-adding enzyme
    • Meso-diaminopimelate-adding enzyme
    • UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
    • UDP-MurNAc-tripeptide synthetase
    • UDP-N-acetylmuramyl-tripeptide synthetase

Gene names

    • Name
      murE
    • ORF names
      IMCC26134_02580

Organism names

Accessions

  • Primary accession
    A0A0E3YVK4

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue264N6-carboxylysine

Post-translational modification

Carboxylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain68-141Mur ligase N-terminal catalytic
Domain154-357Mur ligase central
Domain379-505Mur ligase C-terminal
Motif452-455Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    542
  • Mass (Da)
    58,843
  • Last updated
    2015-06-24 v1
  • Checksum
    F92DD8944635EEE2
MIGYLKQNYPLIHAFAAAAPSACPESEARPRRGSADPFSRALKMAPQLSDLFSEGEIVSMRGTLERPISGLVMDSRRVVPGNVFFALSGLRTDGAVFVAEALSRGAVAIVSAAAPAAAPAKVTYVQVADPRGALARAARRIYREPDRSLGVVGVTGTNGKTTVGHLIKHFLEDGPRVGLLGTISYDLGARIVPSFKTTPEAPDIFGMLAQMRDAGCREAVMEVSSHGIDQQRVDGLEFAAAVFTNLTQDHLDYHQTLEAYFSVKTRLFTGGSGRPPPVAVINIDDNYGRRLLAMLPASVRPVSFGESADASVRAEDVELGFKETVFNLVWPEGRVRVRCSLLGRYNVSNVLAAAATAWGLGRNPQLFLPRLAAFPGVPGRMERIEEGQSYNVLVDYAHTDDALRNALGMLRAITPGRVLCVFGCGGNRDRAKRPLMTRAVEDYADIALPTADNPRNESVVRIFEDMRAGVTQPSKFTWIEDRRRAISLALDMCRPGDCLLVAGKGHETYQEFSDTITPFDDRQIVRELIALKRLRPGAPPPA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP011265
EMBL· GenBank· DDBJ
AKC81942.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp