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InterPro: IPR005720 Dihydroorotate dehydrogenase, class 1, core

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1128 proteins

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

IPR005720 Dihydroorotate_DH_1_core

Type

Domain

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR01037	pyrD_sub1_fam	1128
Signatures in BioMart

InterPro Relationships Help

Found in

IPR012135 Dihydroorotate dehydrogenase, class 1/ 2

GO Term annotation Help

Process

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

Function

GO:0004158 dihydroorotate oxidase activity

Component

GO:0005737 cytoplasm

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, subfamily 2), it is a cytosolic protein while in other eukaryotes it is found in the mitochondria [1].

This describes dihydroorotate dehydrogenases subfamily 1 that includes a number of uncharacterised proteins and a domain of dihydropyrimidine dehydrogenase.

Structural links Help

PDB - click here

SCOP: c.1.4.1 , d.58.1.5

CATH: 2.30.26.10 , 3.20.20.70

Database links Help

Enzyme: EC:1.3.3.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005720

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2RJT9 Dihydroorotate dehydrogenase A

P28272 Dihydroorotate dehydrogenase

Q12882 Dihydropyrimidine dehydrogenase [NADP+]

Q18164 Dihydropyrimidine dehydrogenase [NADP+]

Q8CHR6 Dihydropyrimidine dehydrogenase [NADP+]

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013785	Aldolase-type TIM barrel
IPR009051	Alpha-helical ferredoxin
IPR017896	4Fe-4S ferredoxin, iron-sulpur binding domain
IPR012285	Fumarate reductase, C-terminal
IPR001450	4Fe-4S ferredoxin, iron-sulphur binding, subgroup
IPR001295	Dihydroorotate dehydrogenase, conserved site
IPR017900	4Fe-4S ferredoxin, iron-sulphur binding, conserved site
IPR016040	NAD(P)-binding domain
IPR012135	Dihydroorotate dehydrogenase, class 1/ 2
IPR005720	Dihydroorotate dehydrogenase, class 1, core
IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
IPR001327	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
IPR000759	Adrenodoxin reductase
	PDB Chain
	ModBase
	SWISS-MODEL

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
	Arakaki TL, Buckner FS, Gillespie JR, Malmquist NA, Phillips MA, Kalyuzhniy O, Luft JR, Detitta GT, Verlinde CL, Van Voorhis WC, Hol WG, Merritt EA. Characterization of Trypanosoma brucei dihydroorotate dehydrogenase as a possible drug target; structural, kinetic and RNAi studies. Mol. Microbiol. 68 2008 37-50 [PubMed: 18312275] http://dx.doi.org/10.1111/j.1365-2958.2008.06131.x
	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
	Pinheiro MP, Iulek J, Cristina Nonato M. Crystal structure of Trypanosoma cruzi dihydroorotate dehydrogenase from Y strain. Biochem. Biophys. Res. Commun. 369 2008 812-7 [PubMed: 18302934] http://dx.doi.org/10.1016/j.bbrc.2008.02.074
	Norager S, Arent S, Bjornberg O, Ottosen M, Lo Leggio L, Jensen KF, Larsen S. Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function. J. Biol. Chem. 278 2003 28812-22 [PubMed: 12732650] http://dx.doi.org/10.1074/jbc.M303767200
	Dobritzsch D, Ricagno S, Schneider G, Schnackerz KD, Lindqvist Y. Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer. J. Biol. Chem. 277 2002 13155-66 [PubMed: 11796730] http://dx.doi.org/10.1074/jbc.M111877200

InterPro 23.1