PROSITE documentation PDOC00534Histidinol dehydrogenase signature
Histidinol dehydrogenase (EC 1.1.1.23) (HDH) catalyzes the terminal step in the biosynthesis of histidine in bacteria, fungi, and plants, the four-electron oxidation of L-histidinol to histidine.
In bacteria HDH is a single chain polypeptide; in fungi it is the C-terminal domain of a multifunctional enzyme which catalyzes three different steps of histidine biosynthesis; and in plants it is expressed as nuclear encoded protein precursor which is exported to the chloroplast [1].
As a signature pattern we selected a highly conserved region located in the central part of HDH. This region does not correspond to the part of the enzyme that, in most, but not all HDH sequences contains a cysteine residue which, in Salmonella typhimurium, has been said [2] to be important for the catalytic activity of the enzyme.
Last update:April 2006 / Pattern revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Nagai A. Ward E. Beck J. Tada S. Chang J.-Y. Scheidegger A. Ryals J. |
| Title | Structural and functional conservation of histidinol dehydrogenase between plants and microbes. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 88:4133-4137(1991). | |
| PubMed ID | 2034659 |
| 2 | Authors | Grubmeyer C.T. Gray W.R. |
| Title | A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase. | |
| Source | Biochemistry 25:4778-4784(1986). | |
| PubMed ID | 3533140 |
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