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murD UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 944818, updated on 19-Sep-2024

Summary

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Official Symbol
murD
Official Full Name
UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase
Primary source
ECOCYC:EG10620
Locus tag
b0088
See related
ASAP:ABE-0000318
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0089
Summary
A carbamylated lysine residue is present in the active site. [More information is available at EcoGene: EG10620]. UDP-N-acetylmuramoylalanine-D-glutamate ligase catalyzes the addition of the second amino acid to the peptide moiety of the monomer unit of peptidoglycan. [More information is available at EcoCyc: EG10620].
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Genomic context

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Sequence:
NC_000913.3 (97087..98403)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene peptidoglycan DD-transpeptidase FtsI Neighboring gene UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase Neighboring gene D-alanyl-D-alanine-adding enzyme Neighboring gene phospho-N-acetylmuramoyl-pentapeptide-transferase Neighboring gene peptidoglycan glycosyltransferase FtsW Neighboring gene N-acetylglucosaminyl transferase Neighboring gene UDP-N-acetylmuramate--L-alanine ligase Neighboring gene D-alanine--D-alanine ligase B

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Large-scale preparation, purification, and crystallization of UDP-N-acetylmuramoyl-L-alanine: D-glutamate ligase from Escherichia coli. Auger G, et al. Protein Expr Purif, 1998 Jun. PMID 9631510
  2. Comparison of the D-glutamate-adding enzymes from selected gram-positive and gram-negative bacteria. Walsh AW, et al. J Bacteriol, 1999 Sep. PMID 10464212, Free PMC Article
  3. Role of the ortholog and paralog amino acid invariants in the active site of the UDP-MurNAc-L-alanine:D-glutamate ligase (MurD). Bouhss A, et al. Biochemistry, 1999 Sep 21. PMID 10493791
  4. "Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase. Bertrand JA, et al. J Mol Biol, 2000 Sep 1. PMID 10966819
  5. Phosphinate Inhibitors of the D-Glutamic Acid-Adding Enzyme of Peptidoglycan Biosynthesis. Tanner ME, et al. J Org Chem, 1996 Mar 8. PMID 11667046

See all (44) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. A detailed analysis provides insight into the events that lead to the closure of MurD and reveals that minor structural modifications contribute to major overall conformation alterations.
    Title: Crystallographic Study of Peptidoglycan Biosynthesis Enzyme MurD: Domain Movement Revisited.
  2. Evaluation of three possible reaction pathways leading to tetrahedral intermediate formation by MurD ligase.
    Title: MurD ligase from E. coli: Tetrahedral intermediate formation study by hybrid quantum mechanical/molecular mechanical replica path method.
  3. N-terminus verified by Edman degradation on mature peptide
    Title: Over-production, purification and properties of the uridine diphosphate N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli.
  4. Results report the high resolution crystal structures of MurD in complexes with two novel inhibitors designed to mimic the transition state of the reaction, which contain either the D-Glu or the L-Glu moiety.
    Title: Structural and functional characterization of enantiomeric glutamic acid derivatives as potential transition state analogue inhibitors of MurD ligase.
Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables UDP-N-acetylmuramoylalanine-D-glutamate ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables UDP-N-acetylmuramoylalanine-D-glutamate ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables acid-amino acid ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in cell division IEA
Inferred from Electronic Annotation
more info
  
involved_in cell wall organization IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within peptidoglycan biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in peptidoglycan biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in regulation of cell shape IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase
NP_414630.1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    97087..98403
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_414630.1 UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_414630.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A895NVS9
    Conserved Domains (1) summary
    PRK03806
    Location:1 → 438
    murD; UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
Nucleotide Protein
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