A0A517PMV2 · A0A517PMV2_9PLAN

  • 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 site49UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site128-134ATP (UniProtKB | ChEBI)
Binding site170-171UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site197UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site203UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site205UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site399meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site422-425meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site474meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site478meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functiontetrahydrofolylpolyglutamate synthase activity
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
      HG66A1_25060

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • HG66A1
  • Taxonomic lineage
    Bacteria > Planctomycetota > Planctomycetia > Planctomycetales > Planctomycetaceae > Gimesia

Accessions

  • Primary accession
    A0A517PMV2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue237N6-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
Domain126-328Mur ligase central
Domain350-476Mur ligase C-terminal
Motif422-425Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    513
  • Mass (Da)
    54,821
  • Last updated
    2019-10-16 v1
  • Checksum
    E2B4AD6BB21024F0
MHGSYLTSMSSSSLSLSPGTIAISLRSQFPSASFVDCADICVTSLQSDSRRCQPGDLFVVIAGTRESAEKYIPEAIKNGAKAVLTGRPLTGLEVPQCIVADVRKAYAILCSELADRPSRQLDAVGITGTNGKTTVSWLVRSILQSAGYKAGLTGTVEYHDGNESRPSSLTTPDALELSQLLSAMVKNEVTHSVMEVSSHALDQSRLAGTQLAVAAVTNVTQDHFDYHQNLKNYAACKARIIQHLKPEGTLVLNFDDPVCRSMADGKQSAQKLLTYGLESEADLQVTGIQESAAGTAFEIVFGSDTNSVSTTLIGRHNVSNCLAATAVCLGLGLSLHEIVAGIQALENVPGRMEQVNCGQSCTVLIDYAHTDDALRHAILSARQVCNRRLFCVFGAGGDRDSSKRGLLGIAGSEADRVIITSDNPRSEDPFQIMKAIAAGCQSQGVTPELIEDRKAAIEYALSEAGAGDLVLIAGKGHECEQILRDRKVPFRDRLVVEQYFAEQKISDSQKVSA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP036266
EMBL· GenBank· DDBJ
QDT20717.1
EMBL· GenBank· DDBJ
Genomic DNA

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