Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A174DZL9 · A0A174DZL9_PHOVU

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 site30UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site111-117ATP (UniProtKB | ChEBI)
Binding site153-154UDP-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 site186UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site188UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate (UniProtKB | ChEBI)
Binding site378meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site402-405meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site455meso-2,6-diaminoheptanedioate (UniProtKB | ChEBI)
Binding site459meso-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
      DW105_16170
      , DW193_03790
      , DWX04_12815
      , DXC16_19240
      , DXC44_07700
      , DXD33_17815
      , DXD46_17290
      , ERS852457_01746
      , F9Z94_16690
      , GAY76_00440
      , GAY79_17420
      , HKQ51_05240
      , HUV05_11405
      , KTG10_16550
      , L0N01_17135
      , LI282_14455
      , NCZ15_16175
      , PL594_20495
      , VIC01_04101

Organism names

  • Taxonomic identifier
  • Strains
    • 2789STDY5834842
    • AF18-14
    • AM09-18
    • AM16-6
    • OM08-13BH
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Phocaeicola

Accessions

  • Primary accession
    A0A174DZL9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue220N6-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
Domain22-97Mur ligase N-terminal catalytic
Domain109-305Mur ligase central
Domain327-457Mur ligase C-terminal
Motif402-405Meso-diaminopimelate recognition motif

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    484
  • Mass (Da)
    53,283
  • Last updated
    2016-09-07 v1
  • MD5 Checksum
    7C63D08726BB61521B20E1B0B939E9C2
MKLEKIIKGITVNEIIGDASQEISGINMDSRLIEPGHIFVAVKGTQTDGHTYIQKAIEKGARTVVCENLPETLIENVTYIKVNDTEDVVGKLATTFYGDPTSKLELVGVTGTNGKTTIATLLYNMFRKFGYKTGLISTVCNYIDEEAIPTDHTTPDPITLNKLLGRMADEGCKYAFMEVSSHSVAQKRIGGLKFAGGIFTNLTRDHLDYHKTVENYLKAKKAFFDGLPKTAFALTNLDDKNGLVMTQNTKAKVHTYSLRSLSDFKGKVLEDGFEGMLLDINNVEVNVQFIGRFNASNLLAVYGAACLLGKKTEEVLLALSTLRPVAGRFDSLRSPKGYTAIVDYAHTPDALENVLNAIHEVLNGKGHVITVVGAGGNRDKGKRPLMAQEAVKQSDKVIITSDNPRFEEPQEIINDMLAGLTKEDMRKVISIADRKEAIRTACMLAQAKDVILVAGKGHENYQEIKGIKHHFDDKEVLRDIFANE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CYZI01000007
EMBL· GenBank· DDBJ
CUO31001.1
EMBL· GenBank· DDBJ
Genomic DNA
WCIF01000022
EMBL· GenBank· DDBJ
KAB5434820.1
EMBL· GenBank· DDBJ
Genomic DNA
WDAY01000046
EMBL· GenBank· DDBJ
KAB6557591.1
EMBL· GenBank· DDBJ
Genomic DNA
WDAX01000001
EMBL· GenBank· DDBJ
KAB6577339.1
EMBL· GenBank· DDBJ
Genomic DNA
JAHPYS010000039
EMBL· GenBank· DDBJ
MBU9140318.1
EMBL· GenBank· DDBJ
Genomic DNA
JAJCQG010000047
EMBL· GenBank· DDBJ
MCB7282230.1
EMBL· GenBank· DDBJ
Genomic DNA
JAKNGO010000047
EMBL· GenBank· DDBJ
MCG4690324.1
EMBL· GenBank· DDBJ
Genomic DNA
JAMOYI010000040
EMBL· GenBank· DDBJ
MCM1845919.1
EMBL· GenBank· DDBJ
Genomic DNA
JAQKEI010000038
EMBL· GenBank· DDBJ
MDB0853878.1
EMBL· GenBank· DDBJ
Genomic DNA
JABDSD010000059
EMBL· GenBank· DDBJ
NMX07305.1
EMBL· GenBank· DDBJ
Genomic DNA
JABWDJ010000040
EMBL· GenBank· DDBJ
NVB74116.1
EMBL· GenBank· DDBJ
Genomic DNA
CP043529
EMBL· GenBank· DDBJ
QEW38458.1
EMBL· GenBank· DDBJ
Genomic DNA
QSPP01000072
EMBL· GenBank· DDBJ
RGJ82149.1
EMBL· GenBank· DDBJ
Genomic DNA
QSQC01000034
EMBL· GenBank· DDBJ
RGK10885.1
EMBL· GenBank· DDBJ
Genomic DNA
QSSN01000007
EMBL· GenBank· DDBJ
RGL86880.1
EMBL· GenBank· DDBJ
Genomic DNA
QSTG01000044
EMBL· GenBank· DDBJ
RGM40417.1
EMBL· GenBank· DDBJ
Genomic DNA
QRXI01000016
EMBL· GenBank· DDBJ
RGT91816.1
EMBL· GenBank· DDBJ
Genomic DNA
QRKA01000004
EMBL· GenBank· DDBJ
RHH82118.1
EMBL· GenBank· DDBJ
Genomic DNA
QRMN01000045
EMBL· GenBank· DDBJ
RHJ73849.1
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.
Help