A0A518REK3 · A0A518REK3_9SPHN

  • Protein
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
  • Gene
    murE
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site99-105ATP (UniProtKB | ChEBI)
Binding site141-142UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site168UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site174UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site176UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site372meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site396-399meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site444meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site448meso-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
      FPZ54_07575

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • XS-10
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingomonas

Accessions

  • Primary accession
    A0A518REK3

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue208N6-carboxylysine

Post-translational modification

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

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain16-76Mur ligase N-terminal catalytic
Domain97-299Mur ligase central
Domain322-446Mur ligase C-terminal
Motif396-399Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    471
  • Mass (Da)
    49,568
  • Last updated
    2019-10-16 v1
  • Checksum
    4FCB664A49862DE7
MRLGELTGKGEQDIVTGFAIDHRKVAPGTVFGAFRGTRFNGEEFIPDAIARGAVAVVARPEVKVEGAAHIVSDHPRTEFARIAAKFFAPFPETSVAVTGTNGKTSTVEMVRQLWLMAGHHAASIGTLGVTTASEMVSTGLTTPDVVTFLSNVAGLAREGVTHLAFEASSHGLSQYRTEGLPVRAAAFTNLSRDHLDYHKDMADYFTAKLRLFADVLDPNGVAVVWADDPHSERVIDIARMRGNRIITVGEHGDTIRLVAREPTLLDQKLTIAHGGVEYRVGLPLIGGYQAANALIAAGLVIATGGDPAQTFANLARLQPVRGRLERAAICKSGAPIYVDYAHTPDAIEAAIAALKPHAAGRLIIVFGAGGDRDAGKREPMGLAACTGADLVIVTDDNPREEDAAAIRRQVIKGCPQATEIGDRRAAITAAVAAAGPEDIVLIAGKGHEQGQIVGGMVLPFDDVSVAREAAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP042239
EMBL· GenBank· DDBJ
QDX25897.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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