A0A5E5QC59 · A0A5E5QC59_9GAMM

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 site24UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site26UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site104-110ATP (UniProtKB | ChEBI)
Binding site143UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site144-145UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site171UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site177UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site179UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site360meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site384-387meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site435meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site439meso-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
      BSPWISOX_1537

Organism names

Accessions

  • Primary accession
    A0A5E5QC59

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue211N6-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
Domain19-88Mur ligase N-terminal catalytic
Domain102-288Mur ligase central
Domain313-437Mur ligase C-terminal
Motif384-387Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    474
  • Mass (Da)
    52,874
  • Last updated
    2019-11-13 v1
  • Checksum
    0C5563A7366F7579
MNIQKLLHNITPTNFDFVVQGLCLNSQQVQDGDVFVALQGTTGHGTDYIEQAIDKGCVCILIDSKDIECGVPTIRIDDLSTHLVALAQQMYVDALKVDVIGITGTNGKTSVACFISQLLAHLDIKNGLIGTLGISHSNQHSEQTTPDILTLYRTLDGYRKDGIKTAVLEVSSHGIDQDRIAGLRITHAVFTNLTQDHLDYHQDLKTYQQTKARLFSLASVQFAILNRDDTHYADFLVAAKGKEIIDFGLDDFDDIRPTEQGFLVTLQHHIFEVPFLAKFNLLNVLSVFNTLKTFGFKPEKIIPLLHKLKPPLGRMQKIDNHLIWIDYAHTPDAIENAICTLQQHYPTHDIRVVFGCGGNRDQDKRAKMGKIASKHANTLILTNDNPRNEDPQAIINDILDGIDDSYEVDITLDRQLAIETAVITLGDNECLLIAGKGHETTQIFRDKTIESNDKDIVLAAIIEGIRLKKLKNQQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CABVGN010000053
EMBL· GenBank· DDBJ
VVH61474.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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