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Q5E9W3 (PYRD_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase (quinone), mitochondrial

Short name=DHOdehase
EC=1.3.5.2
Alternative name(s):
Dihydroorotate oxidase
Gene names
Name:DHODH
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. HAMAP-Rule MF_00225

Catalytic activity

(S)-dihydroorotate + a quinone = orotate + a quinol. Ref.3

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP-Rule MF_00225

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP-Rule MF_00225

Subunit structure

Monomer.

Subcellular location

Mitochondrion inner membrane; Single-pass membrane protein By similarity HAMAP-Rule MF_00225.

Post-translational modification

The uncleaved transit peptide is required for mitochondrial targeting and proper membrane integration By similarity. HAMAP-Rule MF_00225

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=9.2 µM for (S)-dihydroorotate Ref.3 Ref.5

KM=13.6 µM for benzyl-(S)-dihydroorotate

KM=19.4 µM for methyl-(S)-dihydroorotate

KM=10.8 µM for quinone Q6

KM=13.2 µM for quinone Q7

Vmax=72 µmol/min/mg enzyme toward (S)-dihydroorotate

Vmax=80 µmol/min/mg enzyme toward benzyl-(S)-dihydroorotate

Vmax=63 µmol/min/mg enzyme toward methyl-(S)-dihydroorotate

Vmax=82 µmol/min/mg enzyme toward quinone Q6

Vmax=88 µmol/min/mg enzyme toward quinone Q7

pH dependence:

Optimum pH is 8.0.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395Dihydroorotate dehydrogenase (quinone), mitochondrial HAMAP-Rule MF_00225
PRO_0000233397
Transit peptide1 – 1010Mitochondrion; not cleaved By similarity

Regions

Topological domain1 – 1010Mitochondrial matrix By similarity
Transmembrane11 – 3020Helical; By similarity
Topological domain31 – 395365Mitochondrial intermembrane By similarity
Nucleotide binding95 – 995FMN By similarity
Nucleotide binding355 – 3562FMN By similarity
Region144 – 1485Substrate binding By similarity
Region211 – 2166Substrate binding By similarity
Region283 – 2842Substrate binding By similarity

Sites

Active site2141Nucleophile By similarity
Binding site991Substrate By similarity
Binding site1191FMN By similarity
Binding site1801FMN By similarity
Binding site2111FMN By similarity
Binding site2541FMN By similarity
Binding site2821FMN; via carbonyl oxygen By similarity
Binding site3051FMN; via amide nitrogen By similarity
Binding site3341FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5E9W3 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 9D093C1641A44BD0

FASTA39542,776
        10         20         30         40         50         60 
MAWRQLKKRA QDAMVILGGG GLLFASYLTA TGDEHFYAEL LMPSLQRLLD PETAHRLAVR 

        70         80         90        100        110        120 
FTSLGLLPRT TFQDSDMLEV RVLGHKFRNP VGIAAGFDKH GEAVDGLYKM GFGFVEIGSV 

       130        140        150        160        170        180 
TPEPQEGNPR PRVFRLPEDQ AIINRYGFNS HGLSVVEHRL RARQQTQARL TEDGLPLGIN 

       190        200        210        220        230        240 
LGKNKTSVDA ASDYAEGVRV LGPLADYLVV NVSSPNTAGL RSLQGKAELR RLLTKVLQER 

       250        260        270        280        290        300 
DALKVAHKPA VLVKIAPDLT AQDKEDIASV VRELGIDGLI VTNSTVSRPA SLQGALRSEP 

       310        320        330        340        350        360 
GGLSGKPLRD LSTQTIREMY ALTQGRVPIV GVGGVSSGQD ALEKIRAGAS LVQLYTALTY 

       370        380        390 
RGPPVVGGVK RELEALLKEQ GFARVTDAIG ADHRR 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Thalamus.
[3]"Purification and properties of the bovine liver mitochondrial dihydroorotate dehydrogenase."
Hines V., Keys L.D. III, Johnston M.
J. Biol. Chem. 261:11386-11392(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[4]Erratum
Hines V., Keys L.D. III, Johnston M.
J. Biol. Chem. 262:15322-15322(1987)
[5]"Analysis of the kinetic mechanism of the bovine liver mitochondrial dihydroorotate dehydrogenase."
Hines V., Johnston M.
Biochemistry 28:1222-1226(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME KINETICS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT020807 mRNA. Translation: AAX08824.1.
BC120337 mRNA. Translation: AAI20338.1.
RefSeqNP_001015650.1. NM_001015650.1.
UniGeneBt.7483.

3D structure databases

ProteinModelPortalQ5E9W3.
SMRQ5E9W3. Positions 30-395.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5E9W3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID533873.
KEGGbta:533873.

Organism-specific databases

CTD1723.

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHOG000225103.
HOVERGENHBG006898.
InParanoidQ5E9W3.
KOK00254.

Enzyme and pathway databases

SABIO-RKQ5E9W3.
UniPathwayUPA00070; UER00946.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00225. DHO_dh_type2.
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01036. pyrD_sub2. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20876177.

Entry information

Entry namePYRD_BOVIN
AccessionPrimary (citable) accession number: Q5E9W3
Secondary accession number(s): Q0P590
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: March 15, 2005
Last modified: February 19, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways