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Protein

Dihydroorotate dehydrogenase (quinone), mitochondrial

Gene

Dhodh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991Substrate
Binding sitei119 – 1191FMN1 Publication
Binding sitei180 – 1801FMN1 Publication
Binding sitei211 – 2111FMN1 Publication
Binding sitei211 – 2111Substrate
Active sitei214 – 2141NucleophileBy similarity
Binding sitei254 – 2541FMN1 Publication
Binding sitei282 – 2821FMN; via carbonyl oxygen1 Publication
Binding sitei305 – 3051FMN; via amide nitrogen1 Publication
Binding sitei334 – 3341FMN; via amide nitrogen1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi95 – 995FMN1 Publication
Nucleotide bindingi355 – 3562FMN1 Publication

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
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BRENDAi1.3.5.2. 5301.
ReactomeiR-RNO-500753. Pyrimidine biosynthesis.
SABIO-RKQ63707.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi68352. Dhodh.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010Mitochondrial intermembrane
Transmembranei11 – 3020HelicalAdd
BLAST
Topological domaini31 – 395365Mitochondrial matrixAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial inner membrane Source: RGD
  • neuronal cell body Source: RGD
  • nucleoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2383.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395Dihydroorotate dehydrogenase (quinone), mitochondrialPRO_0000029886Add
BLAST
Transit peptidei1 – 1010Mitochondrion; not cleaved

Post-translational modificationi

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

Proteomic databases

PaxDbiQ63707.
PRIDEiQ63707.

PTM databases

iPTMnetiQ63707.
PhosphoSiteiQ63707.

Expressioni

Gene expression databases

BgeeiENSRNOG00000015063.
GenevisibleiQ63707. RN.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061315.

Chemistry

BindingDBiQ63707.

Structurei

Secondary structure

1
395
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 394Combined sources
Helixi41 – 488Combined sources
Helixi51 – 6313Combined sources
Helixi76 – 783Combined sources
Beta strandi80 – 823Combined sources
Beta strandi85 – 939Combined sources
Beta strandi101 – 1033Combined sources
Helixi104 – 1096Combined sources
Beta strandi113 – 1208Combined sources
Beta strandi133 – 1364Combined sources
Turni137 – 1404Combined sources
Beta strandi141 – 1444Combined sources
Helixi153 – 16210Combined sources
Helixi164 – 1729Combined sources
Beta strandi177 – 1815Combined sources
Helixi190 – 20112Combined sources
Helixi202 – 2043Combined sources
Beta strandi206 – 2116Combined sources
Helixi226 – 24116Combined sources
Beta strandi243 – 2464Combined sources
Beta strandi250 – 2556Combined sources
Helixi261 – 27414Combined sources
Beta strandi278 – 2814Combined sources
Helixi295 – 2984Combined sources
Beta strandi299 – 3057Combined sources
Helixi306 – 3083Combined sources
Helixi309 – 32214Combined sources
Turni323 – 3253Combined sources
Beta strandi329 – 3346Combined sources
Helixi338 – 3469Combined sources
Beta strandi350 – 3556Combined sources
Helixi356 – 3616Combined sources
Helixi364 – 37916Combined sources
Helixi385 – 3884Combined sources
Helixi391 – 3944Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UUMX-ray2.30A/B30-395[»]
1UUOX-ray2.44A30-395[»]
4ORIX-ray1.50A32-395[»]
ProteinModelPortaliQ63707.
SMRiQ63707. Positions 37-395.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63707.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 1485Substrate binding
Regioni211 – 2166Substrate bindingBy similarity
Regioni283 – 2842Substrate binding

Sequence similaritiesi

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

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

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00225. DHO_dh_type2. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01036. pyrD_sub2. 1 hit.
PROSITEiPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]

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_006255601.2.
XP_008770751.1. XM_008772529.1.
UniGeneiRn.81502.

Genome annotation databases

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

Cross-referencesi

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_006255601.2.
XP_008770751.1. XM_008772529.1.
UniGeneiRn.81502.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UUMX-ray2.30A/B30-395[»]
1UUOX-ray2.44A30-395[»]
4ORIX-ray1.50A32-395[»]
ProteinModelPortaliQ63707.
SMRiQ63707. Positions 37-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000061315.

Chemistry

BindingDBiQ63707.
ChEMBLiCHEMBL2383.

PTM databases

iPTMnetiQ63707.
PhosphoSiteiQ63707.

Proteomic databases

PaxDbiQ63707.
PRIDEiQ63707.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1723.
RGDi68352. Dhodh.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00070; UER00946.
BRENDAi1.3.5.2. 5301.
ReactomeiR-RNO-500753. Pyrimidine biosynthesis.
SABIO-RKQ63707.

Miscellaneous databases

EvolutionaryTraceiQ63707.
PROiQ63707.

Gene expression databases

BgeeiENSRNOG00000015063.
GenevisibleiQ63707. RN.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00225. DHO_dh_type2. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01036. pyrD_sub2. 1 hit.
PROSITEiPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYRD_RAT
AccessioniPrimary (citable) accession number: Q63707
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 7, 2016
This is version 132 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.