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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
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