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ilvE branched-chain-amino-acid aminotransferase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948278, updated on 19-Sep-2024

Summary

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Official Symbol
ilvE
Official Full Name
branched-chain-amino-acid aminotransferase
Primary source
ECOCYC:EG10497
Locus tag
b3770
See related
ASAP:ABE-0012316
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
ECK3762
Summary
Two independent determinations found N-terminal Gly where a Thr is encoded, indicating a modification of Thr to Gly may have occured post-translationally. [More information is available at EcoGene: EG10497]. Branched-chain amino acid transferase (IlvE) is a multifunctional enzyme that carries out the final step in valine, leucine and isoleucine biosyntheses. [More information is available at EcoCyc: EG10497].
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Genomic context

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Sequence:
NC_000913.3 (3952484..3953413)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene uncharacterized protein IlvX Neighboring gene pseudo Neighboring gene acetolactate synthase II subunit IlvM Neighboring gene dihydroxy-acid dehydratase Neighboring gene threonine deaminase

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. Chemoenzymatic synthesis of glutamic acid analogues: substrate specificity and synthetic applications of branched chain aminotransferase from Escherichia coli. Xian M, et al. J Org Chem, 2007 Sep 28. PMID 17718503
  2. The ilvEDA operon of Escherichia coli K12 encodes only one valine-alpha-ketoglutarate transaminase activity. Adams CW, et al. Biochem Biophys Res Commun, 1979 Jul 27. PMID 385001
  3. Isoleucine and valine metabolism in Escherichia coli. V. alpha-Ketoisovaleric acid accumulation. ADELBERG EA, et al. J Biol Chem, 1953 Nov. PMID 13117924
  4. Crystal structures of branched-chain amino acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme. Goto M, et al. Biochemistry, 2003 Apr 8. PMID 12667063
  5. Multivalent regulation of isoleucine-valine transaminase in an Escherichia coli K-12 ilvA deletion strain. Kline EL, et al. J Bacteriol, 1977 May. PMID 400801, Free PMC Article

See all (37) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. N-terminus verified by Edman degradation on mature peptide
    Title: Branched-chain amino acid aminotransferase of Escherichia coli: overproduction and properties.
Submit: New GeneRIF Correction

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 L-isoleucine-2-oxoglutarate transaminase activity IEA
Inferred from Electronic Annotation
more info
  
enables L-leucine-2-oxoglutarate transaminase activity IEA
Inferred from Electronic Annotation
more info
  
enables L-valine-2-oxoglutarate transaminase activity IEA
Inferred from Electronic Annotation
more info
  
enables branched-chain-amino-acid transaminase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables branched-chain-amino-acid transaminase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables branched-chain-amino-acid transaminase activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables transaminase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in L-leucine biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within L-leucine biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in L-leucine biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in L-valine biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within L-valine biosynthetic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in L-valine biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in amino acid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in aspartate biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within aspartate biosynthetic process IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in branched-chain amino acid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in branched-chain amino acid metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in carboxylic acid biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
involved_in isoleucine biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
branched-chain-amino-acid aminotransferase
YP_026247.1

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
    3952484..3953413
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. YP_026247.1 branched-chain-amino-acid aminotransferase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for YP_026247.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A828PFC7
    Conserved Domains (1) summary
    PRK06606
    Location:1 → 307
    PRK06606; branched-chain amino acid transaminase
Nucleotide Protein
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