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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)DescriptionActionsGraphical viewLength
    Binding sitei20FMN; via carbonyl oxygen1 Publication1
    Binding sitei44Substrate1
    Binding sitei128FMN1 Publication1
    Binding sitei128Substrate1
    Active sitei131NucleophileBy similarity1
    Binding sitei133Substrate1
    Binding sitei165FMN1 Publication1
    Binding sitei194FMN; via carbonyl oxygen1 Publication1
    Binding sitei223FMN; via amide nitrogen1 Publication1
    Binding sitei249FMN1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi44 – 45FMN1 Publication2
    Nucleotide bindingi249 – 251FMN1 Publication3
    Nucleotide bindingi272 – 273FMN1 Publication2

    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00004095591 – 313Dihydroorotate dehydrogenase (fumarate)Add BLAST313

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1313
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 7Combined sources3
    Beta strandi10 – 18Combined sources9
    Helixi27 – 35Combined sources9
    Beta strandi41 – 46Combined sources6
    Beta strandi59 – 62Combined sources4
    Beta strandi65 – 68Combined sources4
    Helixi77 – 86Combined sources10
    Turni90 – 92Combined sources3
    Beta strandi95 – 99Combined sources5
    Helixi104 – 121Combined sources18
    Beta strandi124 – 128Combined sources5
    Helixi140 – 142Combined sources3
    Helixi144 – 158Combined sources15
    Beta strandi162 – 166Combined sources5
    Helixi172 – 182Combined sources11
    Beta strandi188 – 193Combined sources6
    Beta strandi197 – 201Combined sources5
    Turni205 – 208Combined sources4
    Beta strandi209 – 211Combined sources3
    Helixi214 – 217Combined sources4
    Beta strandi218 – 223Combined sources6
    Helixi224 – 226Combined sources3
    Helixi227 – 240Combined sources14
    Beta strandi244 – 251Combined sources8
    Helixi255 – 264Combined sources10
    Beta strandi266 – 272Combined sources7
    Helixi273 – 278Combined sources6
    Helixi282 – 297Combined sources16
    Helixi302 – 304Combined sources3
    Turni305 – 307Combined sources3

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ57U83.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni68 – 72Substrate binding5
    Regioni195 – 196Substrate binding2

    Sequence similaritiesi

    Phylogenomic databases

    HOGENOMiHOG000225104.
    InParanoidiQ57U83.
    KOiK00226.
    OMAiNTIENAC.

    Family and domain databases

    CDDicd04741. DHOD_1A_like. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR033886. DHOD_1A.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2B4GX-ray1.95A/B/C/D1-313[»]
    ProteinModelPortaliQ57U83.
    SMRiQ57U83.
    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

    CDDicd04741. DHOD_1A_like. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR033886. DHOD_1A.
    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...

    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: November 30, 2016
    This is version 77 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.