3-hydroxyisobutyrate dehydrogenase (EC 1.1.1.31) catalyzes the NAD-dependent,
reversible oxidation of 3-hydroxbutyrate to methylmalonate [1]. In eukaryotes,
it is a homodimeric mitochondrial protein involved in valine catabolism. In
Pseudomonas aeruginosa [2] (gene mmsB), it is involved in the distal valine
metabolic pathway.
The sequence of 3-hydroxyisobutyrate dehydrogenase from eukaryotic and
prokaryotic sources show that this enzyme has been well conserved throughout
evolution. The following proteins are evolutionary related to 3-hydroxyisobut-yrate dehydrogenase:
- Escherichia coli 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60) (genes
garR and glxR).
- Escherichia coli hypothetical protein ygbJ.
- Escherichia coli hypothetical protein yihU.
- Bacillus subtilis hypothetical protein yfjR.
- Bacillus subtilis hypothetical protein ykwC.
- Mycobacterium tuberculosis hypothetical protein Rv0770.
- Synechocystis strain PCC 6803 hypothetical protein slr0229.
As a signature pattern, we selected a highly conserved glycine-rich region
located at the proteins' N-terminus. This region is probably involved in
binding NAD.
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