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aroA 3-phosphoshikimate 1-carboxyvinyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945528, updated on 23-Apr-2026
Official Symbol
aroA
Official Full Name
3-phosphoshikimate 1-carboxyvinyltransferase
Primary source
ECOCYC:EG10073
Locus tag
b0908
See related
ASAP:ABE-0003095
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0899
Summary
[More information is available at EcoCyc: EG10073].
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Sequence:
NC_000913.3 (958812..960095)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene DUF421 domain-containing protein YcaP Neighboring gene phosphoserine/phosphohydroxythreonine aminotransferase Neighboring gene periplasmic protease YcaL Neighboring gene cytidylate kinase

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. On the mechanism of 5-enolpyruvylshikimate 3-phosphate synthetase. Bondinell WE, et al. J Biol Chem, 1971 Oct 25. PMID 4942558
  2. Identification of the catalytic residues of AroA (Enolpyruvylshikimate 3-phosphate synthase) using partitioning analysis. Mizyed S, et al. Biochemistry, 2003 Jun 17. PMID 12795593
  3. How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli. Eschenburg S, et al. Planta, 2002 Nov. PMID 12430021
  4. A new type of class I bacterial 5-enopyruvylshikimate-3-phosphate synthase mutants with enhanced tolerance to glyphosate. He M, et al. Biochim Biophys Acta, 2001 Nov 7. PMID 11731078
  5. Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail. Schönbrunn E, et al. Proc Natl Acad Sci U S A, 2001 Feb 13. PMID 11171958, Free PMC Article

See all (55) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. A novel 5-enolpyruvylshikimate-3-phosphate synthase shows high glyphosate tolerance in Escherichia coli and tobacco plants.
    Title: A novel 5-enolpyruvylshikimate-3-phosphate synthase shows high glyphosate tolerance in Escherichia coli and tobacco plants.
  2. The results suggest that there is a direct relationship between stability of 5-enolpyruvylshikimate 3-phosphate synthase and pH stability of its folding intermediates
    Title: Acid-induced formation of molten globule states in the wild type Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase and its three mutated forms: G96A, A183T and G96A/A183T.
  3. We identified a novel RPMXR motif that is strictly conserved among class II EPSP synthases and is required for enzymatic acitvity and glyphosate resistance.
    Title: A novel RPMXR motif among class II 5-enolpyruvylshikimate-3-phosphate synthases is required for enzymatic activity and glyphosate resistance.
  4. In an active site that is overwhelmingly positively charged, Asp-313 and Glu-341 side chains of aroA form an "electrostatic sandwich" around the positive charge at C2 in cationic intermediates/transition states, stabilizing them and promoting catalysis.
    Title: Catalytic residues and an electrostatic sandwich that promote enolpyruvyl shikimate 3-phosphate synthase (AroA) catalysis.
  5. analysis of glyphosate resistance resulting from the double mutation Thr97 -> Ile and Pro101 -> Ser in 5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli
    Title: Structural basis of glyphosate resistance resulting from the double mutation Thr97 -> Ile and Pro101 -> Ser in 5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli.
  6. glyphosate ternary complexes of P101S and P101L 5-enolpyruvylshikimate-3-phosphate synthase were determined to between 1.5- and 1.6-A resolution
    Title: Structural basis of glyphosate tolerance resulting from mutations of Pro101 in Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase.
Submit: New GeneRIF Correction

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables 3-phosphoshikimate 1-carboxyvinyltransferase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables 3-phosphoshikimate 1-carboxyvinyltransferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables 3-phosphoshikimate 1-carboxyvinyltransferase activity IEA
Inferred from Electronic Annotation
more info
  
enables catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables transferase activity, transferring alkyl or aryl (other than methyl) groups IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in aromatic amino acid family biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in carboxylic acid metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in chorismate biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within chorismate biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in chorismate biosynthetic process 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 
Preferred Names
3-phosphoshikimate 1-carboxyvinyltransferase
NP_415428.1

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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
    958812..960095
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415428.1 3-phosphoshikimate 1-carboxyvinyltransferase

    See identical proteins and their annotated locations for NP_415428.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    Q7WVX4
    Conserved Domains (1) summary
    cd01554
    Location:12 → 423
    EPT-like; Enol pyruvate transferases family includes EPSP synthases and UDP-N-acetylglucosamine enolpyruvyl transferase. Both enzymes catalyze the reaction of enolpyruvyl transfer.
Nucleotide Protein
Heading Accession and Version

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