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

    Gene ID: 947081, updated on 17-Dec-2024

    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 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 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
    Heading Accession and Version

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