Description

IPR002195 is a Dihydroorotase, conserved site.

<p>This group contains a number of protein families, example are:</p> <ul> <li>Archaeal and bacterial dihydroorotase ([ec:3.5.2.3]) (DHOase)</li> <li>Allantoinase ([ec:3.5.2.5])</li></ul> <p>Dihydroorotase belongs to MEROPS peptidase family M38 (clan MJ), where it is classified as a non-peptidase homologue. DHOase catalyses the third step in the<i>de novo</i>biosynthesis of pyrimidine, the conversion of ureidosuccinic acid (N-carbamoyl-L-aspartate) into dihydroorotate. Dihydroorotase binds a zinc ion which is required for its catalytic activity [[cite:PUB00002652]].</p> <p>In bacteria, DHOase is a dimer of identical chains of about 400 amino-acid residues (gene pyrC) [[cite:PUB00070199]]. In higher eukaryotes, DHOase is part of a large multi-functional protein known as 'rudimentary' in Drosophila melanogaster and CAD in mammals and which catalyzes the first three steps of pyrimidine biosynthesis [[cite:PUB00000720]]. The DHOase domain is located in the central part of this polyprotein. In yeasts, DHOase is encoded by a monofunctional protein (gene URA4). However, a defective DHOase domain [[cite:PUB00001777]] is found in a multifunctional protein (gene URA2) that catalyzes the first two steps of pyrimidine biosynthesis.</p> <p>The comparison of DHOase sequences from various sources shows [[cite:PUB00003725]] that there are two highly conserved regions. The first located in the N-terminal extremity contains two histidine residues suggested [[cite:PUB00001777]] to be involved in binding the zinc ion. The second is found in the C-terminal part. Members of this family of proteins are predicted to adopt a TIM barrel fold [[cite:PUB00004994]].</p> <p>Allantoinase ([ec:3.5.2.5]) is the enzyme that hydrolyzes allantoin into allantoate. In yeast (gene DAL1) [[cite:PUB00005645]], it is the first enzyme in the allantoin degradation pathway; in amphibians [[cite:PUB00002839]] and fishs it catalyzes the second step in the degradation of uric acid. The sequence of allantoinase is evolutionary related to that of DHOases.</p>

This description is obtained from EB-eye REST.

Associated GO terms

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 April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 10

Co-occuring domains 1

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