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Protein

Dihydroorotate dehydrogenase (fumarate)

Gene

Tb927.5.3830

Organism
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro.

Catalytic activityi

(S)-dihydroorotate + fumarate = orotate + succinate.

Cofactori

FMN1 PublicationNote: Binds 1 FMN per subunit.1 Publication

Kineticsi

  1. KM=14 µM for dihydroorotate1 Publication
  2. KM=80 µM for fumarate1 Publication

    pH dependencei

    Optimum pH is 7.8.1 Publication

    Pathwayi: UMP biosynthesis via de novo pathway

    This protein is involved in the pathway UMP biosynthesis via de novo pathway, which is part of Pyrimidine metabolism.
    View all proteins of this organism that are known to be involved in the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei20 – 201FMN; via carbonyl oxygen1 Publication
    Binding sitei44 – 441Substrate
    Binding sitei128 – 1281FMN1 Publication
    Binding sitei128 – 1281Substrate
    Active sitei131 – 1311NucleophileBy similarity
    Binding sitei133 – 1331Substrate
    Binding sitei165 – 1651FMN1 Publication
    Binding sitei194 – 1941FMN; via carbonyl oxygen1 Publication
    Binding sitei223 – 2231FMN; via amide nitrogen1 Publication
    Binding sitei249 – 2491FMN1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi44 – 452FMN1 Publication
    Nucleotide bindingi249 – 2513FMN1 Publication
    Nucleotide bindingi272 – 2732FMN1 Publication

    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

    UniPathwayiUPA00070.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydroorotate dehydrogenase (fumarate) (EC:1.3.98.1)
    Short name:
    DHOD
    Short name:
    DHODase
    Short name:
    DHOdehase
    Alternative name(s):
    Dihydroorotate oxidase
    Gene namesi
    ORF Names:Tb927.5.3830
    OrganismiTrypanosoma brucei brucei (strain 927/4 GUTat10.1)
    Taxonomic identifieri185431 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma
    Proteomesi
    • UP000008524 Componenti: Chromosome 5

    Organism-specific databases

    EuPathDBiTriTrypDB:Tb927.5.3830.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313Dihydroorotate dehydrogenase (fumarate)PRO_0000409559Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    313
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 73Combined sources
    Beta strandi10 – 189Combined sources
    Helixi27 – 359Combined sources
    Beta strandi41 – 466Combined sources
    Beta strandi59 – 624Combined sources
    Beta strandi65 – 684Combined sources
    Helixi77 – 8610Combined sources
    Turni90 – 923Combined sources
    Beta strandi95 – 995Combined sources
    Helixi104 – 12118Combined sources
    Beta strandi124 – 1285Combined sources
    Helixi140 – 1423Combined sources
    Helixi144 – 15815Combined sources
    Beta strandi162 – 1665Combined sources
    Helixi172 – 18211Combined sources
    Beta strandi188 – 1936Combined sources
    Beta strandi197 – 2015Combined sources
    Turni205 – 2084Combined sources
    Beta strandi209 – 2113Combined sources
    Helixi214 – 2174Combined sources
    Beta strandi218 – 2236Combined sources
    Helixi224 – 2263Combined sources
    Helixi227 – 24014Combined sources
    Beta strandi244 – 2518Combined sources
    Helixi255 – 26410Combined sources
    Beta strandi266 – 2727Combined sources
    Helixi273 – 2786Combined sources
    Helixi282 – 29716Combined sources
    Helixi302 – 3043Combined sources
    Turni305 – 3073Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B4GX-ray1.95A/B/C/D1-313[»]
    ProteinModelPortaliQ57U83.
    SMRiQ57U83. Positions 1-313.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ57U83.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni68 – 725Substrate binding
    Regioni195 – 1962Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000225104.
    InParanoidiQ57U83.
    KOiK00226.
    OMAiNTIENAC.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR005720. Dihydroorotate_DH.
    IPR012135. Dihydroorotate_DH_1_2.
    [Graphical view]
    PfamiPF01180. DHO_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000164. DHO_oxidase. 1 hit.
    TIGRFAMsiTIGR01037. pyrD_sub1_fam. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q57U83-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSLKVNILGH EFSNPFMNAA GVLCTTEEDL RRMTESESGS LIGKSCTLAP
    60 70 80 90 100
    RTGNPEPRYF GLPLGSINSM GLPNLGVDFY LSYAAQTHDY SRKPLFLSMS
    110 120 130 140 150
    GLSVEESVEM VKKLAPITKE KGTILELNLS CPNVPGKPQV GYDFDTTRTY
    160 170 180 190 200
    LQKVSEAYGL PFGVKMPPYF DIAHFDMAAA VLNDFPLVKF ITCVNSIGNG
    210 220 230 240 250
    LVIDPANETV VIKPKQGFGG LGGKYVLPTA LANVNAFFRR CPDKLVFGCG
    260 270 280 290 300
    GVYSGEEAFL HILAGASMVQ VGTALHDEGP IIFARLNKEL QEIMTNKGYK
    310
    TLDEFRGRVK TMD
    Length:313
    Mass (Da):34,112
    Last modified:May 10, 2005 - v1
    Checksum:iC005E7470D4C1EA1
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC159455 Genomic DNA. Translation: AAX70836.1.
    CP000068 Genomic DNA. Translation: AAZ11494.1.
    RefSeqiXP_845053.1. XM_839960.1.

    Genome annotation databases

    GeneDBiTb927.5.3830:pep.
    GeneIDi3657493.
    KEGGitbr:Tb927.5.3830.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC159455 Genomic DNA. Translation: AAX70836.1.
    CP000068 Genomic DNA. Translation: AAZ11494.1.
    RefSeqiXP_845053.1. XM_839960.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B4GX-ray1.95A/B/C/D1-313[»]
    ProteinModelPortaliQ57U83.
    SMRiQ57U83. Positions 1-313.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneDBiTb927.5.3830:pep.
    GeneIDi3657493.
    KEGGitbr:Tb927.5.3830.

    Organism-specific databases

    EuPathDBiTriTrypDB:Tb927.5.3830.

    Phylogenomic databases

    HOGENOMiHOG000225104.
    InParanoidiQ57U83.
    KOiK00226.
    OMAiNTIENAC.

    Enzyme and pathway databases

    UniPathwayiUPA00070.

    Miscellaneous databases

    EvolutionaryTraceiQ57U83.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR005720. Dihydroorotate_DH.
    IPR012135. Dihydroorotate_DH_1_2.
    [Graphical view]
    PfamiPF01180. DHO_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000164. DHO_oxidase. 1 hit.
    TIGRFAMsiTIGR01037. pyrD_sub1_fam. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The genome of the African trypanosome Trypanosoma brucei."
      Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H., Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U., Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B., Alsmark U.C.M.
      , Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F., Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C., Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A., Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D., Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D., Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S., Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S., Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G., Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A., Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M., Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S., Walker D., Wanless D., Wang S., White B., White O., Whitehead S., Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E., Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E., Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.
      Science 309:416-422(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 927/4 GUTat10.1Imported.
    2. "Characterization of Trypanosoma brucei dihydroorotate dehydrogenase as a possible drug target; structural, kinetic and RNAi studies."
      Arakaki T.L., Buckner F.S., Gillespie J.R., Malmquist N.A., Phillips M.A., Kalyuzhniy O., Luft J.R., DeTitta G.T., Verlinde C.L.M.J., Van Voorhis W.C., Hol W.G., Merritt E.A.
      Mol. Microbiol. 68:37-50(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH FMN AND OROTATE, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME KINETICS.
      Strain: 927/4 GUTat10.1.

    Entry informationi

    Entry nameiPYRD_TRYB2
    AccessioniPrimary (citable) accession number: Q57U83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 31, 2011
    Last sequence update: May 10, 2005
    Last modified: February 17, 2016
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    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.