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IPR005719 is a Dihydroorotate dehydrogenase, class 2.
<p>This entry represents the enzyme protein dihydroorotate dehydrogenase (also called quinone) exclusively for class 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C terminus. This subfamily has a longer N-terminal region.</p> <p>Dihydroorotate dehydrogenase (DHOD), also known as dihydroorotate oxidase, catalyses the fourth step in de novo pyrimidine biosynthesis, the stereospecific oxidation of (S)-dihydroorotate to orotate, which is the only redox reaction in this pathway. DHODs can be divided into two mains classes: class 1 cytosolic enzymes found primarily in Gram-positive bacteria, and class 2 membrane-associated enzymes found primarily in eukaryotic mitochondria and Gram-negative bacteria [[cite:PUB00033267]].</p> <p>The class 1 DHODs can be further divided into subclasses 1A and 1B, which differ in their structural organisation and use of electron acceptors. The 1A enzyme is a homodimer of two PyrD subunits where each subunit forms a TIM barrel fold with a bound FMN cofactor located near the top of the barrel [[cite:PUB00005052]]. Fumarate is the natural electron acceptor for this enzyme. The 1B enzyme, in contrast is a heterotetramer composed of a central, FMN-containing, PyrD homodimer resembling the 1A homodimer, and two additional PyrK subunits which contain FAD and a 2Fe-2S cluster [[cite:PUB00024613]]. These additional groups allow the enzyme to use NAD(+) as its natural electron acceptor.</p> <p>The class 2 membrane-associated enzymes are monomers which have the FMN-containing TIM barrel domain found in the class 1 PyrD subunit, and an additional N-terminal α helical domain [[cite:PUB00024104], [cite:PUB00033268]]. These enzymes use respiratory quinones as the physiological electron acceptor.</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 |
|---|---|---|---|---|
| Molecular function | Dihydroorotate dehydrogenase activity | Catalysis of the reaction: (S)-dihydroorotate + A = AH(2) + orotate. | ||
| Biological process | 'de novo' pyrimidine nucleobase biosynthetic process | The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors. | ||
| Cellular component | Membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. | ||
| Biological process | Oxidation-reduction process | A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: dihydroorotate dehydrogenase (quinone), mitochondrial-like [Glycine max] gi|356536427|ref|XP_003536739.1| | 17 | ||
| – | PREDICTED: dihydroorotate dehydrogenase (quinone), mitochondrial-like [Glycine max] gi|356536427|ref|XP_003536739.1| | 19 | ||
| – | Dihydroorotate dehydrogenase (Quinone); TAIR: AT5G23300.1 pyrimidine d; Swiss-Prot: sp|P32746|PYRD_ARATH Dihydroorotate dehydrogenase (quinone), mitochondrial; TrEMBL-Plants: tr|I1LF90|I1LF90_SOYBN Dihydroorotate dehydrogenase (quinone), mitochondrial; Found in the gene: LotjaGi5g1v0353100 | 20 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 33.33 |