Nucleotide sequence and characterization of a cDNA encoding the acetohydroxy acid isomeroreductase from Arabidopsis thaliana.
The primary structure of acetohydroxy acid isomeroreductase from Arabidopsis thaliana was deduced from two overlapping cDNA. The full-length cDNA sequence predicts an amino acid sequence for the protein precursor of 591 residues including a putative transit peptide of 67 amino acids. Comparison of the A. thaliana and spinach acetohydroxy acid isomeroreductases reveals that the sequences are conserved in the mature protein regions, but divergent in the transit peptides and around their putative processing site.
Curien
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Unité Mixte CNRS/Rhône-Poulenc Agrochimie, Lyon, France.
Dumas
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Douce
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D015072:2-Acetolactate Mutase / Q000235:genetics*; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics*; D001483:Base Sequence; D016384:Consensus Sequence; D017343:Genes, Plant; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000235:genetics; D016415:Sequence Alignment
D010940:Plant Proteins; D015072:2-Acetolactate Mutase