Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR000807 is a Imidazoleglycerol-phosphate dehydratase.
<p>Imidazoleglycerol-phosphate dehydratase (IGPD; [ec:4.2.1.19]) catalyzes the dehydration of imidazole glycerol phosphate to imidazole acetol phosphate, the sixth step of histidine biosynthesis in plants and microorganisms where the histidine is synthesized de novo. There is an internal repeat in the protein domain that is related by pseudo-dyad symmetry, perhaps as a result of an ancient gene duplication. The apo-form of IGPD exists as a catalytically inactive trimer which, in the presence of specific divalent metal cations such as manganese (Mn2+), cobalt (Co2+), cadmium (Cd2+), nickel (Ni2+), iron (Fe2+) and zinc (Zn2+), assembles to form a biologically active high molecular weight metalloenzyme; a 24-mer with 4-3-2 symmetry. Each 24-mer has 24 active sites, and contains around 1.5 metal ions per monomer, each monomer contributing residues to three separate active sites.</p> <p>IGPD enzymes are monofunctional in fungi, plants, archaea and some eubacteria while they are encoded as bifunctional enzymes in other eubacteria, such that the enzyme is fused to histidinol-phosphate phosphatase, the penultimate enzyme of the histidine biosynthesis pathway. The histidine biosynthesis pathway is a potential target for development of herbicides, and IGPD is a target for the triazole phosphonate herbicides [[cite:PUB00040491], [cite:PUB00022600], [cite:PUB00046135], [cite:PUB00079788], [cite:PUB00079789], [cite:PUB00079790], [cite:PUB00079791], [cite:PUB00079792], [cite:PUB00079793], [cite:PUB00079794], [cite:PUB00079795], [cite:PUB00009674]].</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Biological process | Histidine biosynthetic process | The chemical reactions and pathways resulting in the formation of histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid. | ||
| Molecular function | Imidazoleglycerol-phosphate dehydratase activity | Catalysis of the reaction: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: imidazoleglycerol-phosphate dehydratase-like isoform X2 [Cicer arietinum] gi|502119750|ref|XP_004496726.1| | 13 | ||
| – | Imidazoleglycerol-phosphate dehydratase; TAIR: AT4G14910.1 HISTIDINE BIOSYNTHESIS 5B; Swiss-Prot: sp|Q43072|HIS7_PEA Imidazoleglycerol-phosphate dehydratase; TrEMBL-Plants: tr|I3T3H2|I3T3H2_LOTJA Imidazoleglycerol-phosphate dehydratase; Found in the gene: LotjaGi5g1v0313700 | 14 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 50.00 |