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

Gene ID: 947115, updated on 2-May-2024

Summary

Gene symbol
tyrA
Gene description
fused chorismate mutase/prephenate dehydrogenase
Primary source
ASAP:ABE-0008547
Locus tag
b2600
See related
ECOCYC:EG11039
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
ECK2597
Summary
Bifunctional protein, mutase is N-terminal domain. [More information is available at EcoGene: EG11039]. Bifunctional chorismate mutase / prephenate dehydrogenase (TyrA) carries out the shared first step in the parallel biosynthetic pathways for the aromatic amino acids tyrosine and phenylalanine, as well as the second step in tyrosine biosynthesis. [More information is available at EcoCyc: EG11039].
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Genomic context

Sequence:
NC_000913.3 (2738948..2740069, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene phe operon leader peptide Neighboring gene fused chorismate mutase/prephenate dehydratase Neighboring gene 3-deoxy-7-phosphoheptulonate synthase, Tyr-sensitive Neighboring gene DUF2799 domain-containing lipoprotein YfiL

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables NAD+ binding IBA
Inferred from Biological aspect of Ancestor
more info
 
enables NAD+ binding 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 isomerase activity IEA
Inferred from Electronic Annotation
more info
 
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
 
enables prephenate dehydrogenase (NAD+) activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables prephenate dehydrogenase (NAD+) activity IDA
Inferred from Direct Assay
more info
PubMed 
enables prephenate dehydrogenase (NAD+) activity IEA
Inferred from Electronic Annotation
more info
 
enables prephenate dehydrogenase (NADP+) activity IEA
Inferred from Electronic Annotation
more info
 
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within L-phenylalanine biosynthetic process IDA
Inferred from Direct Assay
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
 
involved_in tyrosine biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
 
acts_upstream_of_or_within tyrosine biosynthetic process IDA
Inferred from Direct Assay
more info
PubMed 
involved_in tyrosine biosynthetic process IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 

General protein information

Preferred Names
fused chorismate mutase/prephenate dehydrogenase
NP_417091.1

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
    2738948..2740069 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417091.1 fused chorismate mutase/prephenate dehydrogenase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417091.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S7FEI1
    Conserved Domains (1) summary
    PRK11199
    Location:1373
    tyrA; bifunctional chorismate mutase/prephenate dehydrogenase; Provisional