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Protein

Dihydroorotate dehydrogenase (quinone), mitochondrial

Gene

DHODH

Organism
Bos taurus (Bovine)
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.1 Publication

Cofactori

FMNBy similarityNote: Binds 1 FMN per subunit.By similarity

Kineticsi

  1. KM=9.2 µM for (S)-dihydroorotate2 Publications
  2. KM=13.6 µM for benzyl-(S)-dihydroorotate2 Publications
  3. KM=19.4 µM for methyl-(S)-dihydroorotate2 Publications
  4. KM=10.8 µM for quinone Q62 Publications
  5. KM=13.2 µM for quinone Q72 Publications
  1. Vmax=72 µmol/min/mg enzyme toward (S)-dihydroorotate2 Publications
  2. Vmax=80 µmol/min/mg enzyme toward benzyl-(S)-dihydroorotate2 Publications
  3. Vmax=63 µmol/min/mg enzyme toward methyl-(S)-dihydroorotate2 Publications
  4. Vmax=82 µmol/min/mg enzyme toward quinone Q62 Publications
  5. Vmax=88 µmol/min/mg enzyme toward quinone Q72 Publications

pH dependencei

Optimum pH is 8.0.2 Publications

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), 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 sitei99SubstrateBy similarity1
Binding sitei119FMNBy similarity1
Binding sitei180FMNBy similarity1
Binding sitei211FMNBy similarity1
Active sitei214NucleophileBy similarity1
Binding sitei254FMNBy similarity1
Binding sitei282FMN; via carbonyl oxygenBy similarity1
Binding sitei305FMN; via amide nitrogenBy similarity1
Binding sitei334FMN; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi95 – 99FMNBy similarity5
Nucleotide bindingi355 – 356FMNBy similarity2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

SABIO-RKQ5E9W3.
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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 10Mitochondrial matrixBy similarity10
Transmembranei11 – 30HelicalBy similarityAdd BLAST20
Topological domaini31 – 395Mitochondrial intermembraneBy similarityAdd BLAST365

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002333971 – 395Dihydroorotate dehydrogenase (quinone), mitochondrialAdd BLAST395
Transit peptidei1 – 10Mitochondrion; not cleavedBy similarity10

Post-translational modificationi

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

Proteomic databases

PaxDbiQ5E9W3.
PRIDEiQ5E9W3.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000055859.

Structurei

3D structure databases

ProteinModelPortaliQ5E9W3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 148Substrate bindingBy similarity5
Regioni211 – 216Substrate bindingBy similarity6
Regioni283 – 284Substrate bindingBy similarity2

Sequence similaritiesi

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1436. Eukaryota.
COG0167. LUCA.
HOGENOMiHOG000225103.
HOVERGENiHBG006898.
InParanoidiQ5E9W3.
KOiK00254.

Family and domain databases

CDDicd04738. DHOD_2_like. 1 hit.
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.

Q5E9W3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWRQLKKRA QDAMVILGGG GLLFASYLTA TGDEHFYAEL LMPSLQRLLD
60 70 80 90 100
PETAHRLAVR FTSLGLLPRT TFQDSDMLEV RVLGHKFRNP VGIAAGFDKH
110 120 130 140 150
GEAVDGLYKM GFGFVEIGSV TPEPQEGNPR PRVFRLPEDQ AIINRYGFNS
160 170 180 190 200
HGLSVVEHRL RARQQTQARL TEDGLPLGIN LGKNKTSVDA ASDYAEGVRV
210 220 230 240 250
LGPLADYLVV NVSSPNTAGL RSLQGKAELR RLLTKVLQER DALKVAHKPA
260 270 280 290 300
VLVKIAPDLT AQDKEDIASV VRELGIDGLI VTNSTVSRPA SLQGALRSEP
310 320 330 340 350
GGLSGKPLRD LSTQTIREMY ALTQGRVPIV GVGGVSSGQD ALEKIRAGAS
360 370 380 390
LVQLYTALTY RGPPVVGGVK RELEALLKEQ GFARVTDAIG ADHRR
Length:395
Mass (Da):42,776
Last modified:March 15, 2005 - v1
Checksum:i9D093C1641A44BD0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020807 mRNA. Translation: AAX08824.1.
BC120337 mRNA. Translation: AAI20338.1.
RefSeqiNP_001015650.1. NM_001015650.1.
UniGeneiBt.7483.

Genome annotation databases

GeneIDi533873.
KEGGibta:533873.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020807 mRNA. Translation: AAX08824.1.
BC120337 mRNA. Translation: AAI20338.1.
RefSeqiNP_001015650.1. NM_001015650.1.
UniGeneiBt.7483.

3D structure databases

ProteinModelPortaliQ5E9W3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000055859.

Proteomic databases

PaxDbiQ5E9W3.
PRIDEiQ5E9W3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi533873.
KEGGibta:533873.

Organism-specific databases

CTDi1723.

Phylogenomic databases

eggNOGiKOG1436. Eukaryota.
COG0167. LUCA.
HOGENOMiHOG000225103.
HOVERGENiHBG006898.
InParanoidiQ5E9W3.
KOiK00254.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00946.
SABIO-RKQ5E9W3.

Family and domain databases

CDDicd04738. DHOD_2_like. 1 hit.
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_BOVIN
AccessioniPrimary (citable) accession number: Q5E9W3
Secondary accession number(s): Q0P590
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: March 15, 2005
Last modified: October 5, 2016
This is version 80 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.