A0A9D5RKK9 · A0A9D5RKK9_9FIRM

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.
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial 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

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Cell wall biogenesis; peptidoglycan biosynthesis.

Features

Showing features for binding site, active site, site.

Type
IDPosition(s)Description
Binding site30UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site110-116ATP (UniProtKB | ChEBI)
Binding site151UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site152-153UDP-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 site187UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site380meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site404-407meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site456meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site460meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site496substrate
Binding site551substrate
Active site560
Active site560Proton donor
Binding site561-562substrate
Binding site652substrate
Site654Could be important to modulate the pK values of the two catalytic cysteine residues
Binding site685substrate
Site703Could be important to modulate the pK values of the two catalytic cysteine residues
Binding site703-704substrate
Active site712Proton acceptor
Binding site713-714substrate

GO annotations

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

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • 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
  • Recommended name
    Diaminopimelate epimerase
  • EC number
  • Short names
    DAP epimerase
  • Alternative names
    • PLP-independent amino acid racemase

Gene names

    • Name
      murE
    • Synonyms
      dapF
    • ORF names
      E7269_00350

Organism names

Accessions

  • Primary accession
    A0A9D5RKK9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue221N6-carboxylysine

Post-translational modification

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

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, motif.

Type
IDPosition(s)Description
Domain23-95Mur ligase N-terminal catalytic
Domain108-309Mur ligase central
Domain331-458Mur ligase C-terminal
Motif404-407Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.
Belongs to the diaminopimelate epimerase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    769
  • Mass (Da)
    84,898
  • Last updated
    2023-05-03 v1
  • Checksum
    EFCA6B02CCDA00B2
MLLKELLSEITYEVLQGTTDTDVTELVYDSRKASVGCVFLCISGTTVDAHDFIPQVAEKGAAAIVVTKDVQVPANVTVVKVENARKALSYMAAAYFGKPAEKMTLIGITGTKGKTTTSYMVQAMLEMAGKKVGVIGTIGAVIDKGIVKTSNTTPESYEVQRLFAKMVEAGCEYCIMEVSSQGMKMDRVAGVLFDYGIFTNFSSDHIGPNEHADMAEYLYCKSLLFRQCKVGIINRDSEYWQGVTEGHTCELKTYGFDADADLRGANQKLVRKSGVLGVEFDVEGVLNCHVKTCIPGRFSVYNCLTALAIGWHLDIPIEAMTHALKNIRVPGRVELVDISPKFTIMVDYAHNAMSVESLLTTIKEYNPNRIICVYGLGGNRSKVRRYEVGELCGKMADLSVLTADNPRNEEIADIFNDIKIGLAKTNGKYIEIPDRKEAIYYAIDHAQENDIIVVFGKGHEDYQEIKGVRYPYNDKEAILSYLKREMNFVKLHGCGNPYIYMDVRGKNYENAFLQALSIKVSDKSKGIGADGLIVLDDAQTEGTDGRMRMFNADGSEGAMCGNGIRCLAKFMYEHAGIEKEHMVIETKSGLREVDLIHEGDEITKATVYMGHPEFEAANVPVISEHPVFMDGELPVELESGVKYCGTCMSMGNPHCVIFTEDIDALELAKIGPKFECHEMFPERVNTEFIEIVDRNNVRMRVWERGSGETMACGTGACAVVAAGVRTGRLSNKVNVMMRGGTLEITYDVENNDIYMTGEAVQICVGKLRV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SVEO01000001
EMBL· GenBank· DDBJ
MBE5921199.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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