Description

IPR038494 is a Imidazole glycerol phosphate dehydratase domain superfamily.

<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.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 1

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: