|PROSITE documentation PDOC00534|
Histidinol dehydrogenase (EC 220.127.116.11) (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 .
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  to be important for the catalytic activity of the enzyme.Last update:
April 2006 / Pattern revised.
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).|
|2||Authors||Grubmeyer C.T., Gray W.R.|
|Title||A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase.|