Homoserine dehydrogenase (EC 1.1.1.3) (HDh) [1,2] catalyzes NAD-dependent
reduction of aspartate β-semialdehyde into homoserine. This reaction is
the third step in a pathway leading from aspartate to homoserine. The latter
participates in the biosynthesis of threonine and then isoleucine as well as
in that of methionine.
HDh is found either as a single chain protein as in some bacteria and yeast,
or as a bifunctional enzyme consisting of an N-terminal aspartokinase domain
and a C-terminal HDh domain as in bacteria such as Escherichia coli and in
plants.
As a signature pattern, we selected the best conserved region of Hdh. This is
a segment of 23 to 24 residues located in the central section and that
contains two conserved aspartate residues.
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