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    murQ N-acetylmuramic acid 6-phosphate etherase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946893, updated on 3-Dec-2024

    Summary

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    Official Symbol
    murQ
    Official Full Name
    N-acetylmuramic acid 6-phosphate etherase
    Primary source
    ECOCYC:G7263
    Locus tag
    b2428
    See related
    ASAP:ABE-0008007
    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
    ECK2423; yfeU
    Summary
    A lyase-type cleavage mechanism is proposed for MurQ. [More information is available at EcoGene: EG14162]. MurQ catalyzes the cleavage of the lactyl ether moiety of N-acetylmuramic acid 6-phosphate (MurNAc-6-P), acting in one of the pathways that recycle murein components . [More information is available at EcoCyc: G7263].
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    Genomic context

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    Sequence:
    NC_000913.3 (2545773..2546669)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene oxidoreductase UcpA Neighboring gene DNA-binding transcriptional dual regulator MurR Neighboring gene N-acetylmuramic acid-specific PTS enzyme IICB component/anhydro-N-acetylmuramic acid transporter Neighboring gene penicillin binding protein 4B

    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. Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling. Hadi T, et al. Biochemistry, 2008 Nov 4. PMID 18837509
    2. The transcriptional factors MurR and catabolite activator protein regulate N-acetylmuramic acid catabolism in Escherichia coli. Jaeger T, et al. J Bacteriol, 2008 Oct. PMID 18723630, Free PMC Article
    3. An alternative route for recycling of N-acetylglucosamine from peptidoglycan involves the N-acetylglucosamine phosphotransferase system in Escherichia coli. Plumbridge J. J Bacteriol, 2009 Sep. PMID 19617367, Free PMC Article
    4. Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography. Fountoulakis M, et al. Electrophoresis, 1999 Aug. PMID 10493123
    5. Identification of a phosphotransferase system of Escherichia coli required for growth on N-acetylmuramic acid. Dahl U, et al. J Bacteriol, 2004 Apr. PMID 15060041, Free PMC Article

    See all (11) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Putative active site acid/base residues are probed by mutagenesis, and Glu83 and Glu114 are found to be crucial for catalysis.
      Title: Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling.
    2. Escherichia coli MurQ etherase has a role in cleaving the lactyl ether bond of N-acetylmuramic acid
      Title: Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase".
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables carbohydrate derivative binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables carbon-oxygen lyase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables carbon-oxygen lyase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables carbon-oxygen lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ether hydrolase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ether hydrolase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables lyase 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 1,6-anhydro-N-acetyl-beta-muramic acid catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in N-acetylmuramic acid catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in amino sugar catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in amino sugar catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within amino sugar catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in amino sugar metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in peptidoglycan turnover IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in peptidoglycan turnover IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within peptidoglycan turnover IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    N-acetylmuramic acid 6-phosphate etherase
    NP_416923.1

    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
      2545773..2546669
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416923.1 N-acetylmuramic acid 6-phosphate etherase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416923.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A775YWC6
      Conserved Domains (1) summary
      TIGR00274
      Location:6 → 296
      TIGR00274; N-acetylmuramic acid 6-phosphate etherase
    Nucleotide Protein
    Heading Accession and Version

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