C1A0Y0 · C1A0Y0_RHOE4

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 site57UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site148-154ATP (UniProtKB | ChEBI)
Binding site190-191UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site217UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site225UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site425meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site449-452meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site505meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site509meso-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
    • Ordered locus names
      RER_35570

Organism names

Accessions

  • Primary accession
    C1A0Y0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue257N6-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 region, domain, motif.

TypeIDPosition(s)Description
Region1-20Disordered
Domain52-132Mur ligase N-terminal catalytic
Domain146-354Mur ligase central
Domain376-507Mur ligase C-terminal
Motif449-452Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    544
  • Mass (Da)
    57,195
  • Last updated
    2009-05-26 v1
  • Checksum
    02C57687F164A449
MPNRLQSSNSDGAPGTRPTQPVATAITALSELSGARLEWVGQPGSQSSEVVVKGVDLRAQGIVADDLFAALPGARTHGAQFAVDALGRGATAILTDEAGLELIEAAGKAPDRSVPVLVHPNPRDVLGEISAEIYGRPSEKMQVVGITGTSGKTTTSYLLEAAIAGAGRKPGLVGTIETRIDGRRVPSALTTPEAPQLHALFAVMAEQGIDTVVMEVSSHALALGRVDGIRFDIGAFTNLSQDHLDFHRDFEEYFQAKARLFDPESTVRAEHAVVCVDDVWGRRMAELAATDESDAVTTVSTSTAEAEWKVGAVEVAEDGSQTFELVGPDGQSWPVSLRLPGRYNVANAALALTVSFAAGLDPDAAVRALGTVDVPGRVQRIDRGQSFLAVVDYAHKPAALEAVIATLRNQVPGRVAVVVGAGGDRDAGKRTLMGEAGARGADLLIVTDDNPRTEDPAKIRASVMQGAIDVPESERGEIREVGDRALAIEQAVRWAQPGDVVLVAGKGHEVGQEIDGVKHPFDDREVLGEMIGRFAINTAHGGKQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP008957
EMBL· GenBank· DDBJ
BAH34265.1
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