PROSITE documentation PDOC006973-hydroxyisobutyrate dehydrogenase signature
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.
Last update:December 2001 / Pattern and text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Rougraff P.M. Zhang B. Kuntz M.J. Harris R.A. Crabb D.W. |
| Title | Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to other pyridine nucleotide-dependent dehydrogenases. | |
| Source | J. Biol. Chem. 264:5899-5903(1989). | |
| PubMed ID | 2647728 |
| 2 | Authors | Steele M.I. Lorenz D. Hatter K. Park A. Sokatch J.R. |
| Title | Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase. | |
| Source | J. Biol. Chem. 267:13585-13592(1992). | |
| PubMed ID | 1339433 |
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