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InterPro: IPR001295 Dihydroorotate dehydrogenase, conserved site

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2050 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession

IPR001295 Dihydroorotate_DH_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00911	DHODEHASE_1	1551
PROSITE pattern	PS00912	DHODEHASE_2	1848
Signatures in BioMart

InterPro Relationships Help

Found in

IPR005719 Dihydroorotate dehydrogenase, class 2
IPR012135 Dihydroorotate dehydrogenase, class 1/ 2
IPR013785 Aldolase-type TIM barrel

GO Term annotation Help

Process

GO:0006207 'de novo' pyrimidine base biosynthetic process
GO:0055114 oxidation reduction

Function

GO:0004152 dihydroorotate dehydrogenase activity

InterPro annotation

Entry Details in BioMart

Abstract

Dihydroorotate dehydrogenase (EC:1.3.3.1) (DHOdehase) catalyzes the fourth step in the de novo biosynthesis of pyrimidine, the conversion of dihydroorotate into orotate. DHOdehase is a ubiquitous FAD flavoprotein. In bacteria (gene pyrD), DHOdease is located on the inner side of the cytosolic membrane. In some yeasts, such as in Saccharomyces cerevisiae (gene URA1), it is a cytosolic protein while in other eukaryotes it is found in the mitochondria [1].

Structural links Help

PDB - click here

SCOP: c.1.4.1

CATH: 2.30.26.10 , 3.20.20.70

Database links Help

PDBe-motif: PS00911 , PS00912

Enzyme: EC:1.3

PROSITE doc: PDOC00708

PANDIT: PF01180

Blocks: IPB001295

COMe: PRX000411

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001295

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O35435 Dihydroorotate dehydrogenase, mitochondrial

P28272 Dihydroorotate dehydrogenase

P32746 Dihydroorotate dehydrogenase, mitochondrial

P32748 Dihydroorotate dehydrogenase, mitochondrial

Q02127 Dihydroorotate dehydrogenase, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013785	Aldolase-type TIM barrel
IPR005719	Dihydroorotate dehydrogenase, class 2
IPR012135	Dihydroorotate dehydrogenase, class 1/ 2
IPR005720	Dihydroorotate dehydrogenase, class 1, core
IPR001295	Dihydroorotate dehydrogenase, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Nagy M, Lacroute F, Thomas D. Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts. Proc. Natl. Acad. Sci. U.S.A. 89 8966-70 1992 [PubMed: 1409592] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=1409592

Additional Reading Open in usermanual
	Hurt DE, Widom J, Clardy J. Structure of Plasmodium falciparum dihydroorotate dehydrogenase with a bound inhibitor. Acta Crystallogr. D Biol. Crystallogr. 62 2006 312-23 [PubMed: 16510978] http://dx.doi.org/10.1107/S0907444905042642
	Wolfe AE, Thymark M, Gattis SG, Fagan RL, Hu YC, Johansson E, Arent S, Larsen S, Palfey BA. Interaction of benzoate pyrimidine analogues with class 1A dihydroorotate dehydrogenase from Lactococcus lactis. Biochemistry 46 2007 5741-53 [PubMed: 17444658] http://dx.doi.org/10.1021/bi7001554
	Walse B, Dufe VT, Svensson B, Fritzson I, Dahlberg L, Khairoullina A, Wellmar U, Al-Karadaghi S. The structures of human dihydroorotate dehydrogenase with and without inhibitor reveal conformational flexibility in the inhibitor and substrate binding sites. Biochemistry 47 2008 8929-36 [PubMed: 18672895] http://dx.doi.org/10.1021/bi8003318
	Baumgartner R, Walloschek M, Kralik M, Gotschlich A, Tasler S, Mies J, Leban J. Dual binding mode of a novel series of DHODH inhibitors. J. Med. Chem. 49 2006 1239-47 [PubMed: 16480261] http://dx.doi.org/10.1021/jm0506975
	Hurt DE, Sutton AE, Clardy J. Brequinar derivatives and species-specific drug design for dihydroorotate dehydrogenase. Bioorg. Med. Chem. Lett. 16 2006 1610-5 [PubMed: 16406782] http://dx.doi.org/10.1016/j.bmcl.2005.12.029

InterPro 23.1