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Q5E9W3

- PYRD_BOVIN

UniProt

Q5E9W3 - PYRD_BOVIN

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Protein

Dihydroorotate dehydrogenase (quinone), mitochondrial

Gene
DHODH
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

(S)-dihydroorotate + a quinone = orotate + a quinol.1 Publication

Cofactori

Binds 1 FMN per subunit By similarity.UniRule annotation

Kineticsi

  1. KM=9.2 µM for (S)-dihydroorotate2 Publications
  2. KM=13.6 µM for benzyl-(S)-dihydroorotate
  3. KM=19.4 µM for methyl-(S)-dihydroorotate
  4. KM=10.8 µM for quinone Q6
  5. 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 dependencei

Optimum pH is 8.0.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991Substrate By similarity
Binding sitei119 – 1191FMN By similarity
Binding sitei180 – 1801FMN By similarity
Binding sitei211 – 2111FMN By similarity
Active sitei214 – 2141Nucleophile By similarity
Binding sitei254 – 2541FMN By similarity
Binding sitei282 – 2821FMN; via carbonyl oxygen By similarity
Binding sitei305 – 3051FMN; via amide nitrogen By similarity
Binding sitei334 – 3341FMN; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi95 – 995FMN By similarity
Nucleotide bindingi355 – 3562FMN By similarity

GO - Molecular functioni

  1. dihydroorotate oxidase activity Source: InterPro

GO - Biological processi

  1. 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
  2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
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
ProteomesiUP000009136: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010Mitochondrial matrix By similarity
Transmembranei11 – 3020Helical; By similarityAdd
BLAST
Topological domaini31 – 395365Mitochondrial intermembrane By similarityAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial inner membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395Dihydroorotate dehydrogenase (quinone), mitochondrialUniRule annotationPRO_0000233397Add
BLAST
Transit peptidei1 – 1010Mitochondrion; not cleaved By similarity

Post-translational modificationi

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

Proteomic databases

PRIDEiQ5E9W3.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliQ5E9W3.
SMRiQ5E9W3. Positions 30-395.

Family & Domainsi

Region

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

Sequence similaritiesi

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0167.
HOGENOMiHOG000225103.
HOVERGENiHBG006898.
InParanoidiQ5E9W3.
KOiK00254.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00225. DHO_dh_type2.
InterProiIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000164. DHO_oxidase. 1 hit.
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

MAWRQLKKRA QDAMVILGGG GLLFASYLTA TGDEHFYAEL LMPSLQRLLD    50
PETAHRLAVR FTSLGLLPRT TFQDSDMLEV RVLGHKFRNP VGIAAGFDKH 100
GEAVDGLYKM GFGFVEIGSV TPEPQEGNPR PRVFRLPEDQ AIINRYGFNS 150
HGLSVVEHRL RARQQTQARL TEDGLPLGIN LGKNKTSVDA ASDYAEGVRV 200
LGPLADYLVV NVSSPNTAGL RSLQGKAELR RLLTKVLQER DALKVAHKPA 250
VLVKIAPDLT AQDKEDIASV VRELGIDGLI VTNSTVSRPA SLQGALRSEP 300
GGLSGKPLRD LSTQTIREMY ALTQGRVPIV GVGGVSSGQD ALEKIRAGAS 350
LVQLYTALTY RGPPVVGGVK RELEALLKEQ GFARVTDAIG ADHRR 395
Length:395
Mass (Da):42,776
Last modified:March 15, 2005 - v1
Checksum:i9D093C1641A44BD0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BT020807 mRNA. Translation: AAX08824.1 .
BC120337 mRNA. Translation: AAI20338.1 .
RefSeqi NP_001015650.1. NM_001015650.1.
UniGenei Bt.7483.

3D structure databases

ProteinModelPortali Q5E9W3.
SMRi Q5E9W3. Positions 30-395.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5E9W3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 533873.
KEGGi bta:533873.

Organism-specific databases

CTDi 1723.

Phylogenomic databases

eggNOGi COG0167.
HOGENOMi HOG000225103.
HOVERGENi HBG006898.
InParanoidi Q5E9W3.
KOi K00254.

Enzyme and pathway databases

UniPathwayi UPA00070 ; UER00946 .
SABIO-RK Q5E9W3.

Miscellaneous databases

NextBioi 20876177.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00225. DHO_dh_type2.
InterProi IPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view ]
Pfami PF01180. DHO_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsi TIGR01036. pyrD_sub2. 1 hit.
PROSITEi PS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

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: February 19, 2014
This is version 68 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

External Data

Dasty 3

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