A0A7Y9NB16 · A0A7Y9NB16_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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site103-109ATP (UniProtKB | ChEBI)
Binding site145-146UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site172UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site178UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site180UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site376meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site400-403meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site448meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site452meso-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
      HDC29_003812

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • JAI108
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingopyxis

Accessions

  • Primary accession
    A0A7Y9NB16

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue212N6-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.

Type
IDPosition(s)Description
Domain19-75Mur ligase N-terminal catalytic
Domain101-303Mur ligase central
Domain326-450Mur ligase C-terminal
Motif400-403Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    479
  • Mass (Da)
    49,704
  • Last updated
    2021-06-02 v1
  • MD5 Checksum
    BF908349E3103E8F9FBE6BF59097880C
MRLAALLEDQALEGSGPVVTGLAIDHRKVAPGTVFGAFVGEKFNGEDFIPAALEAGAVAIVARPEARVEGAVHVADANPRRAFAHIAARFFHRFPATCVAVTGTNGKTSTVEMTRQLWRMAGFNAASIGTLGITTSMDSASTGLTTPDIVTFLSNMSGLAAEGVTHAAFEASSHGLDQYRTEGLPVKAAAFTNLSHDHLDYHGTMDSYLSAKLRLFTEVVEPGGAAVVGADDEYSPAVIGAARARGVRLLTVGTRGEALRLVSREATQLGQSLVITAGDLSQKVDLPLIGGYQVANALVSAGLVIATGGDARQTLANLARLQPVRGRLERAAITRAGAPVYVDYAHTPDAIEAALDALRPHAAGRLILVFGAGGDRDQAKRPEMGRVAAAKADVLVITDDNPRGEDPAAIRDAIAAAAPGARVIGDRRAAIAAAIAEARGDDIVCIAGKGHEQGQIVGRGDEMRVIPFDDVAVAREEAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACCCJ010000006
EMBL· GenBank· DDBJ
NYF34202.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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