aroE

168

5-enolpyruvyl-shikimate-3-phosphate (EPSP) synthase, 3-phosphoshikimate 1-carboxyvinyltransferase

Locus: BSU_22600

Molecular weight: 45.08 kDa

Isoelectric point: 6.34

Protein length: 428 aa

Gene length: 1287 bp

Function: biosynthesis of aromatic amino acids

Product: 5-enolpyruvyl-shikimate-3-phosphate (EPSP) synthase

Essential: yes

E.C.: 2.5.1.19

Synonyms: aroE

Genomic Context

Hide small RNAsZoom:

List of homologs in different organisms, belongs to COG0128 (Galperin et al., 2021)

Gene

Coordinates: 2,367,954 → 2,369,240

Phenotypes of a mutant

• essential on LB medium PubMed, but not on BHI medium PubMed
• the mutant is able to grow on LB if menachinone is added to the medium PubMed

The protein

Catalyzed reaction/ biological activity

• 3-phosphoshikimate + phosphoenolpyruvate --> 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate (according to UniProt)

Protein family

• EPSP synthase family (with MurAA and MurAB, according to UniProt)

Structure

• 3RMT (PDB) (from B. halodurans, 68% identity, 87% similarity)
• P20691 (AlphaFold)

Effectors of protein activity

• inhibited by glyphosate PubMed

Expression and Regulation

Operons

• Genes: trpE-trpD-trpC-trpF-trpB-trpA-hisC-tyrA-aroE

  Description: PubMed

  Regulation

  • not expressed if tryptophan is available (MtrB) PubMed
  • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

  Regulatory mechanism

  • MtrB: transcription termination, PubMed, in mtrB regulon

• Genes: hisC-tyrA-aroE

  Description: PubMed

  Additional information

  • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Biological materials

Mutant

• BKE22600 (ΔaroE::erm  trpC2) available at BGSC and in Jörg Stülke's lab,  PubMed, upstream reverse: _UP1_CTTATCTCGTTTCATTTTTT,  downstream forward: _UP4_TGAAGTTTTACTTCAGGATT

Expression vectors

• for expression in B. subtilis, in pBQ200: piGEM2,  available in Fabian Commichau's lab

Labs working on this gene/protein

• Fabian Commichau, Göttingen, Germany homepage

References

Reviews

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Original Publications

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