SubtiBank SubtiBank
pheA
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pheA

prephenate dehydratase
Locus
BSU_27900
Isoelectric point
5.89
Molecular weight
31.75 kDa
Protein length
285 aa Sequence Blast
Gene length
858 bp Sequence Blast
Function
biosynthesis of phenylalanine
Product
prephenate dehydratase
Essential
no
E.C.
4.2.1.51
Synonyms
Outlinks
KEGGBsubCycSubtiListUniProtExpression Browser

Genomic Context

      
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Categories containing this gene/protein

  • Metabolism → Amino acid/ nitrogen metabolism → Biosynthesis/ acquisition of amino acids → Biosynthesis/ acquisition of aromatic amino acids

    • Gene

    Coordinates
    2,851,283 → 2,852,140

    The protein

    Catalyzed reaction/ biological activity

  • H+ + prephenate --> 3-phenylpyruvate + CO2 + H2O (according to UniProt)

    • Domains

  • Prephenate dehydratase domain (aa 2-183) (according to UniProt)
  • ACT domain (aa 204-281) (according to UniProt)

    • Effectors of protein activity

  • subject to feedback inhibtion by phenylalanine PubMed

    • Structure

  • 4LUB (from Streptococcus mutans, 42% identity)

    • Expression and Regulation

    Operons

    Genes
    spo0B-obg-thrR-pheA
    Description
    PubMed

    Sigma factors

  • SigA: sigma factor, PubMed, in SigA regulon

    • Additional information

  • expression is repressed by binding of RpoE to the A-rich sequence in the -35 region of the promoter PubMed
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    Biological materials

    Mutant

  • 1A617 ( pheA::erm), PubMed, available at BGSC
  • BKE27900 (ΔpheA::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_GACTTTCATGACGATTTTCT, downstream forward: _UP4_TAAAAAAAGCCCACTAGAGG
  • BKK27900 (ΔpheA::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_GACTTTCATGACGATTTTCT, downstream forward: _UP4_TAAAAAAAGCCCACTAGAGG

    • References

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