{PDOC00697} {PS00895; 3_HYDROXYISOBUT_DH} {BEGIN} ************************************************ * 3-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. -Consensus pattern: [LIVMFY](2)-G-L-G-x-[MQ]-G-x(2)-[MA]-[SAV]-x-[SNHR] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2001 / Pattern and text revised. [ 1] Rougraff P.M., Zhang B., Kuntz M.J., Harris R.A., Crabb D.W. "Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to other pyridine nucleotide-dependent dehydrogenases." J. Biol. Chem. 264:5899-5903(1989). PubMed=2647728 [ 2] Steele M.I., Lorenz D., Hatter K., Park A., Sokatch J.R. "Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase." J. Biol. Chem. 267:13585-13592(1992). PubMed=1339433 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}