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PROSITE documentation PDOC00534

Histidinol dehydrogenase signature

Description:

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.

Technical section:

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

HISOL_DEHYDROGENASE, PS00611Histidinol dehydrogenase signature  (PATTERN)
Consensus pattern: [IVTPM] - [DEG] - x(2,3) - [AYEPQ] - G - [PT] - [ST] - [ED] - [LIVSTA] - [LIVMAECGFT] - [LIVMA] - [LIVMAYF] - [ACNDSTI] - x(2,3) - [ACNGVST] - x(4,6) - [LIVMAC] - [AVLKIT] - [SACLYWNRMTV] - [DEG] - [LIVMFCA] - [LIVMKFR] - [SAGVI] - x(2) - E - H
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE
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Matching PDB structures: 1K75 1KAE 1KAH 1KAR [ALL]

References:

1 AuthorsNagai A., Ward E., Beck J., Tada S., Chang J.-Y., Scheidegger A., Ryals J.
TitleStructural and functional conservation of histidinol dehydrogenase between plants and microbes.
SourceProc. Natl. Acad. Sci. U.S.A. 88:4133-4137(1991).
PubMed ID2034659
2 AuthorsGrubmeyer C.T., Gray W.R.
TitleA cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase.
SourceBiochemistry 25:4778-4784(1986).
PubMed ID3533140

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