We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00738Imidazoleglycerol-phosphate dehydratase signatures
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00738
Description
Imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) is the enzyme that catalyzes the seventh step in the biosynthesis of histidine in bacteria, fungi and plants. In most organisms it is a monofunctional protein of about 22 to 29 Kd. In some bacteria such as Escherichia coli it is the C-terminal domain of a bifunctional protein that include a histidinol-phosphatase domain [1].
We developed two signature patterns that each include two consecutive histidine residues.
Last update:April 2006 / Pattern revised.
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Technical section
PROSITE methods (with tools and information) covered by this documentation:
Reference
| 1 | Authors | Carlomagno M.S. Chiariotti L. Alifano P. Nappo A.G. Bruni C.B. |
| Title | Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons. | |
| Source | J. Mol. Biol. 203:585-606(1988). | |
| PubMed ID | 3062174 |
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