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pheA fused chorismate mutase/prephenate dehydratase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947081, updated on 26-Mar-2025

Summary

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Official Symbol
pheA
Official Full Name
fused chorismate mutase/prephenate dehydratase
Primary source
ECOCYC:EG10707
Locus tag
b2599
See related
ASAP:ABE-0008545
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
ECK2596
Summary
The N-terminal end of this bifunctional protein specifies the chorismate mutase activity while the remainder of the sequence specifies the second enzymatic activity, prephenate dehydratase. [More information is available at EcoCyc: EG10707].
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Genomic context

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Sequence:
NC_000913.3 (2737745..2738905)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene ribosome-associated inhibitor A Neighboring gene ncRNA Neighboring gene phe operon leader peptide Neighboring gene fused chorismate mutase/prephenate dehydrogenase Neighboring gene 3-deoxy-7-phosphoheptulonate synthase, Tyr-sensitive

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. Novel mutations in the pheA gene of Escherichia coli K-12 which result in highly feedback inhibition-resistant variants of chorismate mutase/prephenate dehydratase. Nelms J, et al. Appl Environ Microbiol, 1992 Aug. PMID 1514806, Free PMC Article
  2. New insight into the catalytic mechanism of chorismate mutases from structural studies. Lee AY, et al. Chem Biol, 1995 Apr. PMID 9383421
  3. Exhaustive mutagenesis of six secondary active-site residues in Escherichia coli chorismate mutase shows the importance of hydrophobic side chains and a helix N-capping position for stability and catalysis. Lassila JK, et al. Biochemistry, 2007 Jun 12. PMID 17506527
  4. Kinetic studies on the mechanism of chorismate mutase/prephenate dehydratase from Escherichia coli K12. Baldwin GS, et al. Biochim Biophys Acta, 1983 Jan 26. PMID 6337635
  5. Construction from Mu d1 (lac Apr) lysogens of lambda bacteriophage bearing promoter-lac fusions: isolation of lambda ppheA-lac. Gowrishankar J, et al. J Bacteriol, 1982 Jun. PMID 6281237, Free PMC Article

See all (48) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The wild-type enzyme binds phenylalanine in a kinetically selective manner; no other amino acids tested appeared to bind the enzyme in the early time frame examined.
    Title: Redesigning the PheA domain of gramicidin synthetase leads to a new understanding of the enzyme's mechanism and selectivity.
  2. Computationally predicted chorismate mutase mutant Ala32Ser shows increased catalytic efficiency.
    Title: Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity.
Submit: New GeneRIF Correction

Pathways from PubChem

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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 catalytic activity IEA
Inferred from Electronic Annotation
more info
  
enables chorismate mutase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables chorismate mutase activity IEA
Inferred from Electronic Annotation
more info
  
enables chorismate mutase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables hydro-lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables isomerase activity IEA
Inferred from Electronic Annotation
more info
  
enables lyase activity IEA
Inferred from Electronic Annotation
more info
  
enables prephenate dehydratase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables prephenate dehydratase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables prephenate dehydratase activity IEA
Inferred from Electronic Annotation
more info
  
enables prephenate dehydratase activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in L-phenylalanine biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in L-phenylalanine biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within L-phenylalanine biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in amino acid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
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 metabolic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within tyrosine biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
fused chorismate mutase/prephenate dehydratase
NP_417090.1

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
    2737745..2738905
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417090.1 fused chorismate mutase/prephenate dehydratase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417090.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    C7EXK8
    Conserved Domains (1) summary
    PRK10622
    Location:1 → 386
    pheA; bifunctional chorismate mutase/prephenate dehydratase; Provisional
Nucleotide Protein
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