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    glmU fused N-acetylglucosamine-1-phosphate uridyltransferase and glucosamine-1-phosphate acetyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948246, updated on 17-Dec-2024

    Summary

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    Official Symbol
    glmU
    Official Full Name
    fused N-acetylglucosamine-1-phosphate uridyltransferase and glucosamine-1-phosphate acetyltransferase
    Primary source
    ECOCYC:EG11198
    Locus tag
    b3730
    See related
    ASAP:ABE-0012201
    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
    ECK3723; yieA
    Summary
    GlmU contains 22 hexapeptide repeats. [More information is available at EcoGene: EG11198]. glmU encodes a fused enzyme with two enzymatic activities that catalyze sequential steps in the biosynthesis of UDP-N-acetyl-D-glucosamine (UDP-GlcNAc), an essential precursor of cell wall peptidoglycan, lipopolysaccharide and enterobacterial common antigen . [More information is available at EcoCyc: EG11198].
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    Genomic context

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    Sequence:
    NC_000913.3 (3913830..3915200, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene phosphate ABC transporter periplasmic binding protein Neighboring gene L-glutamine--D-fructose-6-phosphate aminotransferase Neighboring gene ATP synthase F1 complex subunit epsilon Neighboring gene ATP synthase F1 complex subunit beta

    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. Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products. Olsen LR, et al. Protein Sci, 2007 Jun. PMID 17473010, Free PMC Article
    2. Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth. Pompeo F, et al. J Biol Chem, 2001 Feb 9. PMID 11084021
    3. Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily. Brown K, et al. EMBO J, 1999 Aug 2. PMID 10428949, Free PMC Article
    4. Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes. Pompeo F, et al. J Bacteriol, 1998 Sep. PMID 9733680, Free PMC Article
    5. Overexpression, one-step purification and characterization of UDP-glucose dehydrogenase and UDP-N-acetylglucosamine pyrophosphorylase. De Luca C, et al. Bioorg Med Chem, 1996 Jan. PMID 8689233

    See all (31) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 UDP-N-acetylglucosamine diphosphorylase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables UDP-N-acetylglucosamine diphosphorylase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables acyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables acyltransferase activity, transferring groups other than amino-acyl groups IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables glucosamine-1-phosphate N-acetyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables glucosamine-1-phosphate N-acetyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables magnesium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables nucleotidyltransferase 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 UDP-N-acetylglucosamine biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within UDP-N-acetylglucosamine biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in cell morphogenesis IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in cell wall organization IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in lipid A biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    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 IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    fused N-acetylglucosamine-1-phosphate uridyltransferase and glucosamine-1-phosphate acetyltransferase
    NP_418186.1

    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
      3913830..3915200 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418186.1 fused N-acetylglucosamine-1-phosphate uridyltransferase and glucosamine-1-phosphate acetyltransferase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418186.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376MF39, A0A8S7RCA3
      Conserved Domains (1) summary
      PRK09451
      Location:1 → 456
      glmU; bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU
    Nucleotide Protein
    Heading Accession and Version

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