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Protein

Dihydroorotate dehydrogenase (quinone), mitochondrial

Gene

Dhodh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.

Catalytic activityi

(S)-dihydroorotate + a quinone = orotate + a quinol.

Cofactori

FMN1 PublicationNote: Binds 1 FMN per subunit.1 Publication

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes orotate from (S)-dihydroorotate (quinone route).
Proteins known to be involved in this subpathway in this organism are:
  1. Dihydroorotate dehydrogenase (quinone), mitochondrial (Dhodh)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes orotate from (S)-dihydroorotate (quinone route), the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei99Substrate1
Binding sitei119FMN1 Publication1
Binding sitei180FMN1 Publication1
Binding sitei211FMN1 Publication1
Binding sitei211Substrate1
Active sitei214NucleophileBy similarity1
Binding sitei254FMN1 Publication1
Binding sitei282FMN; via carbonyl oxygen1 Publication1
Binding sitei305FMN; via amide nitrogen1 Publication1
Binding sitei334FMN; via amide nitrogen1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi95 – 99FMN1 Publication5
Nucleotide bindingi355 – 356FMN1 Publication2

GO - Molecular functioni

  • dihydroorotate dehydrogenase activity Source: RGD
  • drug binding Source: RGD
  • FMN binding Source: RGD
  • ubiquinone binding Source: RGD

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: RGD
  • 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  • female pregnancy Source: RGD
  • lactation Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • regulation of mitochondrial fission Source: RGD
  • response to caffeine Source: RGD
  • response to drug Source: RGD
  • response to L-arginine Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to starvation Source: RGD

Keywordsi

Molecular functionOxidoreductase
Biological processPyrimidine biosynthesis
LigandFlavoprotein, FMN

Enzyme and pathway databases

BRENDAi1.3.5.2 5301
ReactomeiR-RNO-500753 Pyrimidine biosynthesis
SABIO-RKiQ63707
UniPathwayiUPA00070; UER00946

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroorotate dehydrogenase (quinone), mitochondrial (EC:1.3.5.2)
Short name:
DHOdehase
Alternative name(s):
Dihydroorotate oxidase
Gene namesi
Name:Dhodh
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi68352 Dhodh

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 10Mitochondrial intermembrane10
Transmembranei11 – 30HelicalAdd BLAST20
Topological domaini31 – 395Mitochondrial matrixAdd BLAST365

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2383

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000298861 – 395Dihydroorotate dehydrogenase (quinone), mitochondrialAdd BLAST395
Transit peptidei1 – 10Mitochondrion; not cleaved10

Post-translational modificationi

The uncleaved transit peptide is required for mitochondrial targeting and proper membrane integration.

Proteomic databases

PaxDbiQ63707
PRIDEiQ63707

PTM databases

iPTMnetiQ63707
PhosphoSitePlusiQ63707

Expressioni

Gene expression databases

BgeeiENSRNOG00000015063
GenevisibleiQ63707 RN

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061315

Chemistry databases

BindingDBiQ63707

Structurei

Secondary structure

1395
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 39Combined sources4
Helixi41 – 48Combined sources8
Helixi51 – 63Combined sources13
Helixi76 – 78Combined sources3
Beta strandi80 – 82Combined sources3
Beta strandi85 – 93Combined sources9
Beta strandi101 – 103Combined sources3
Helixi104 – 109Combined sources6
Beta strandi113 – 120Combined sources8
Beta strandi133 – 136Combined sources4
Turni137 – 140Combined sources4
Beta strandi141 – 144Combined sources4
Helixi153 – 162Combined sources10
Helixi164 – 172Combined sources9
Beta strandi177 – 181Combined sources5
Helixi190 – 201Combined sources12
Helixi202 – 204Combined sources3
Beta strandi206 – 211Combined sources6
Helixi226 – 241Combined sources16
Beta strandi243 – 246Combined sources4
Beta strandi250 – 255Combined sources6
Helixi261 – 274Combined sources14
Beta strandi278 – 281Combined sources4
Helixi295 – 298Combined sources4
Beta strandi299 – 305Combined sources7
Helixi306 – 308Combined sources3
Helixi309 – 322Combined sources14
Turni323 – 325Combined sources3
Beta strandi329 – 334Combined sources6
Helixi338 – 346Combined sources9
Beta strandi350 – 355Combined sources6
Helixi356 – 361Combined sources6
Helixi364 – 379Combined sources16
Helixi385 – 388Combined sources4
Helixi391 – 394Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UUMX-ray2.30A/B30-395[»]
1UUOX-ray2.44A30-395[»]
4ORIX-ray1.50A32-395[»]
ProteinModelPortaliQ63707
SMRiQ63707
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63707

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 148Substrate binding5
Regioni211 – 216Substrate bindingBy similarity6
Regioni283 – 284Substrate binding2

Sequence similaritiesi

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1436 Eukaryota
COG0167 LUCA
GeneTreeiENSGT00500000044924
HOGENOMiHOG000225103
HOVERGENiHBG006898
InParanoidiQ63707
KOiK00254
OMAiLQNAMGF
OrthoDBiEOG091G07JK
PhylomeDBiQ63707
TreeFamiTF105973

Family and domain databases

CDDicd04738 DHOD_2_like, 1 hit
Gene3Di3.20.20.70, 1 hit
HAMAPiMF_00225 DHO_dh_type2, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR005720 Dihydroorotate_DH
IPR005719 Dihydroorotate_DH_2
IPR001295 Dihydroorotate_DH_CS
PfamiView protein in Pfam
PF01180 DHO_dh, 1 hit
TIGRFAMsiTIGR01036 pyrD_sub2, 1 hit
PROSITEiView protein in PROSITE
PS00911 DHODEHASE_1, 1 hit
PS00912 DHODEHASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q63707-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWRQLRKRA LDAVIILGGG GLLFTSYLTA TGDDHFYAEY LMPGLQRLLD
60 70 80 90 100
PESAHRLAVR VTSLGLLPRA TFQDSDMLEV KVLGHKFRNP VGIAAGFDKN
110 120 130 140 150
GEAVDGLYKL GFGFVEVGSV TPQPQEGNPR PRVFRLPEDQ AVINRYGFNS
160 170 180 190 200
HGLSVVEHRL RARQQKQAQL TADGLPLGIN LGKNKTSEDA AADYAEGVRT
210 220 230 240 250
LGPLADYLVV NVSSPNTAGL RSLQGKTELR HLLSKVLQER DALKGTRKPA
260 270 280 290 300
VLVKIAPDLT AQDKEDIASV ARELGIDGLI VTNTTVSRPV GLQGALRSET
310 320 330 340 350
GGLSGKPLRD LSTQTIREMY ALTQGRIPII GVGGVSSGQD ALEKIQAGAS
360 370 380 390
LVQLYTALIF LGPPVVVRVK RELEALLKER GFTTVTDAIG ADHRR
Length:395
Mass (Da):42,663
Last modified:November 1, 1996 - v1
Checksum:i4C7E1A9C5E5E60EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80778 mRNA Translation: CAA56765.1
PIRiA59277 S47435
RefSeqiNP_001008553.1, NM_001008553.1
XP_006255663.1, XM_006255601.3
XP_008770751.1, XM_008772529.2
UniGeneiRn.81502

Genome annotation databases

EnsembliENSRNOT00000066733; ENSRNOP00000061315; ENSRNOG00000015063
GeneIDi65156
KEGGirno:65156
UCSCiRGD:68352 rat

Similar proteinsi

Entry informationi

Entry nameiPYRD_RAT
AccessioniPrimary (citable) accession number: Q63707
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 140 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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