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PROSITE documentation PDOC00697 [for PROSITE entry PS00895]

3-hydroxyisobutyrate dehydrogenase signature





Description

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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Technical section

PROSITE method (with tools and information) covered by this documentation:

3_HYDROXYISOBUT_DH, PS00895; 3-hydroxyisobutyrate dehydrogenase signature  (PATTERN)


References

1AuthorsRougraff P.M. Zhang B. Kuntz M.J. Harris R.A. Crabb D.W.
TitleCloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to other pyridine nucleotide-dependent dehydrogenases.
SourceJ. Biol. Chem. 264:5899-5903(1989).
PubMed ID2647728

2AuthorsSteele M.I. Lorenz D. Hatter K. Park A. Sokatch J.R.
TitleCharacterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate dehydrogenase.
SourceJ. Biol. Chem. 267:13585-13592(1992).
PubMed ID1339433



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