Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5E9W3

- PYRD_BOVIN

UniProt

Q5E9W3 - PYRD_BOVIN

Protein

Dihydroorotate dehydrogenase (quinone), mitochondrial

Gene

DHODH

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    Vmax=72 µmol/min/mg enzyme toward (S)-dihydroorotate2 Publications

    Vmax=80 µmol/min/mg enzyme toward benzyl-(S)-dihydroorotate2 Publications

    Vmax=63 µmol/min/mg enzyme toward methyl-(S)-dihydroorotate2 Publications

    Vmax=82 µmol/min/mg enzyme toward quinone Q62 Publications

    Vmax=88 µmol/min/mg enzyme toward quinone Q72 Publications

    pH dependencei

    Optimum pH is 8.0.2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei99 – 991SubstrateBy similarity
    Binding sitei119 – 1191FMNBy similarity
    Binding sitei180 – 1801FMNBy similarity
    Binding sitei211 – 2111FMNBy similarity
    Active sitei214 – 2141NucleophileBy similarity
    Binding sitei254 – 2541FMNBy similarity
    Binding sitei282 – 2821FMN; via carbonyl oxygenBy similarity
    Binding sitei305 – 3051FMN; via amide nitrogenBy similarity
    Binding sitei334 – 3341FMN; via amide nitrogenBy similarity

    Regions

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

    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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 395395Dihydroorotate dehydrogenase (quinone), mitochondrialPRO_0000233397Add
    BLAST
    Transit peptidei1 – 1010Mitochondrion; not cleavedBy similarity

    Post-translational modificationi

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

    Proteomic databases

    PRIDEiQ5E9W3.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5E9W3.
    SMRiQ5E9W3. Positions 30-395.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1010Mitochondrial matrixBy similarity
    Topological domaini31 – 395365Mitochondrial intermembraneBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 3020HelicalBy similarityAdd
    BLAST

    Family & Domainsi

    Region

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

    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: October 1, 2014
    This is version 69 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