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Protein

Dihydroorotate dehydrogenase (quinone), mitochondrial

Gene

PFF0160c

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

FMN3 PublicationsNote: Binds 1 FMN per subunit.3 Publications

Kineticsi

  1. KM=13.1 µM for 2,3-dimethoxy-5-methyl-6-(3-methyl-2-butenyl)-1,4-benzoquinone (CoQ1)1 Publication

    Pathwayi: UMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes orotate from (S)-dihydroorotate (quinone route).
    Proteins known to be involved in this subpathway in this organism are:
    1. Dihydroorotate dehydrogenase (quinone), mitochondrial (PFF0160c)
    This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes orotate from (S)-dihydroorotate (quinone route), the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei229Substrate1
    Binding sitei249FMN2 Publications1
    Binding sitei342FMN2 Publications1
    Binding sitei342Substrate1
    Active sitei345NucleophileBy similarity1
    Binding sitei347Substrate1
    Binding sitei429FMN2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi225 – 229FMN2 Publications5
    Nucleotide bindingi477 – 478FMN2 Publications2
    Nucleotide bindingi505 – 507FMN2 Publications3
    Nucleotide bindingi528 – 529FMN2 Publications2

    GO - Molecular functioni

    • dihydroorotate dehydrogenase activity Source: GeneDB

    GO - Biological processi

    • 'de novo' pyrimidine nucleobase biosynthetic process Source: GeneDB
    • 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
    • response to drug Source: GeneDB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Keywords - Ligandi

    Flavoprotein, FMN

    Enzyme and pathway databases

    ReactomeiR-PFA-500753. Pyrimidine biosynthesis.
    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
    ORF Names:PFF0160c
    OrganismiPlasmodium falciparum (isolate 3D7)
    Taxonomic identifieri36329 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)
    Proteomesi
    • UP000001450 Componenti: Chromosome 6

    Organism-specific databases

    EuPathDBiPlasmoDB:PF3D7_0603300.

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transmembranei143 – 163HelicalSequence analysisAdd BLAST21

    GO - Cellular componenti

    • integral component of membrane Source: UniProtKB-KW
    • mitochondrial inner membrane Source: GeneDB
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL3588732.
    DrugBankiDB01117. Atovaquone.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 23MitochondrionSequence analysisAdd BLAST23
    ChainiPRO_000002988824 – 569Dihydroorotate dehydrogenase (quinone), mitochondrialAdd BLAST546

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Chemistry databases

    BindingDBiQ08210.

    Structurei

    Secondary structure

    1569
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi166 – 178Combined sources13
    Helixi181 – 193Combined sources13
    Helixi206 – 208Combined sources3
    Beta strandi210 – 212Combined sources3
    Beta strandi215 – 223Combined sources9
    Turni225 – 230Combined sources6
    Beta strandi231 – 233Combined sources3
    Helixi234 – 238Combined sources5
    Turni239 – 241Combined sources3
    Beta strandi243 – 250Combined sources8
    Beta strandi263 – 266Combined sources4
    Turni267 – 270Combined sources4
    Beta strandi271 – 274Combined sources4
    Helixi283 – 299Combined sources17
    Helixi301 – 303Combined sources3
    Beta strandi307 – 312Combined sources6
    Helixi321 – 332Combined sources12
    Helixi333 – 335Combined sources3
    Beta strandi337 – 342Combined sources6
    Beta strandi346 – 348Combined sources3
    Helixi351 – 355Combined sources5
    Helixi357 – 377Combined sources21
    Helixi412 – 415Combined sources4
    Beta strandi418 – 422Combined sources5
    Beta strandi425 – 430Combined sources6
    Helixi436 – 449Combined sources14
    Beta strandi452 – 456Combined sources5
    Helixi467 – 469Combined sources3
    Beta strandi474 – 478Combined sources5
    Helixi479 – 481Combined sources3
    Helixi482 – 495Combined sources14
    Turni496 – 498Combined sources3
    Beta strandi502 – 507Combined sources6
    Helixi511 – 520Combined sources10
    Beta strandi522 – 528Combined sources7
    Helixi529 – 534Combined sources6
    Helixi535 – 537Combined sources3
    Helixi538 – 552Combined sources15
    Helixi558 – 561Combined sources4
    Helixi564 – 566Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1TV5X-ray2.40A158-569[»]
    3I65X-ray2.00A158-569[»]
    3I68X-ray2.40A158-569[»]
    3I6RX-ray2.50A158-569[»]
    3O8AX-ray2.30A158-569[»]
    3SFKX-ray2.95A158-569[»]
    4CQ8X-ray1.98A/B158-569[»]
    4CQ9X-ray2.72A/B158-569[»]
    4CQAX-ray2.82A/B158-569[»]
    4ORMX-ray2.07A158-569[»]
    4RX0X-ray2.25A158-569[»]
    5BOOX-ray2.80A/B158-569[»]
    5DELX-ray2.20A158-569[»]
    5FI8X-ray2.32A158-569[»]
    5TBOX-ray2.15A158-569[»]
    ProteinModelPortaliQ08210.
    SMRiQ08210.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ08210.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni274 – 278Substrate binding5
    Regioni458 – 459Substrate binding2

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOGENOMiHOG000225103.
    InParanoidiQ08210.
    KOiK00254.
    OMAiLMPLGRT.
    PhylomeDBiQ08210.

    Family and domain databases

    CDDicd04738. DHOD_2_like. 1 hit.
    Gene3Di3.20.20.70. 2 hits.
    InterProiIPR013785. Aldolase_TIM.
    IPR005720. Dihydroorotate_DH.
    IPR005719. Dihydroorotate_DH_2.
    IPR001295. Dihydroorotate_DH_CS.
    [Graphical view]
    PfamiPF01180. DHO_dh. 1 hit.
    [Graphical view]
    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.

    Q08210-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MISKLKPQFM FLPKKHILSY CRKDVLNLFE QKFYYTSKRK ESNNMKNESL
    60 70 80 90 100
    LRLINYNRYY NKIDSNNYYN GGKILSNDRQ YIYSPLCEYK KKINDISSYV
    110 120 130 140 150
    SVPFKINIRN LGTSNFVNNK KDVLDNDYIY ENIKKEKSKH KKIIFLLFVS
    160 170 180 190 200
    LFGLYGFFES YNPEFFLYDI FLKFCLKYID GEICHDLFLL LGKYNILPYD
    210 220 230 240 250
    TSNDSIYACT NIKHLDFINP FGVAAGFDKN GVCIDSILKL GFSFIEIGTI
    260 270 280 290 300
    TPRGQTGNAK PRIFRDVESR SIINSCGFNN MGCDKVTENL ILFRKRQEED
    310 320 330 340 350
    KLLSKHIVGV SIGKNKDTVN IVDDLKYCIN KIGRYADYIA INVSSPNTPG
    360 370 380 390 400
    LRDNQEAGKL KNIILSVKEE IDNLEKNNIM NDESTYNEDN KIVEKKNNFN
    410 420 430 440 450
    KNNSHMMKDA KDNFLWFNTT KKKPLVFVKL APDLNQEQKK EIADVLLETN
    460 470 480 490 500
    IDGMIISNTT TQINDIKSFE NKKGGVSGAK LKDISTKFIC EMYNYTNKQI
    510 520 530 540 550
    PIIASGGIFS GLDALEKIEA GASVCQLYSC LVFNGMKSAV QIKRELNHLL
    560
    YQRGYYNLKE AIGRKHSKS
    Length:569
    Mass (Da):65,558
    Last modified:February 1, 1995 - v1
    Checksum:i88880384EBD52FE3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L15446 Unassigned DNA. Translation: AAC37170.1.
    AL844505 Genomic DNA. Translation: CAG25203.1.
    RefSeqiXP_966023.1. XM_960930.1.

    Genome annotation databases

    EnsemblProtistsiCAG25203; CAG25203; PF3D7_0603300.
    GeneDBiPF3D7_0603300.1:pep.
    GeneIDi3885966.
    KEGGipfa:PFF0160c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L15446 Unassigned DNA. Translation: AAC37170.1.
    AL844505 Genomic DNA. Translation: CAG25203.1.
    RefSeqiXP_966023.1. XM_960930.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1TV5X-ray2.40A158-569[»]
    3I65X-ray2.00A158-569[»]
    3I68X-ray2.40A158-569[»]
    3I6RX-ray2.50A158-569[»]
    3O8AX-ray2.30A158-569[»]
    3SFKX-ray2.95A158-569[»]
    4CQ8X-ray1.98A/B158-569[»]
    4CQ9X-ray2.72A/B158-569[»]
    4CQAX-ray2.82A/B158-569[»]
    4ORMX-ray2.07A158-569[»]
    4RX0X-ray2.25A158-569[»]
    5BOOX-ray2.80A/B158-569[»]
    5DELX-ray2.20A158-569[»]
    5FI8X-ray2.32A158-569[»]
    5TBOX-ray2.15A158-569[»]
    ProteinModelPortaliQ08210.
    SMRiQ08210.
    ModBaseiSearch...
    MobiDBiSearch...

    Chemistry databases

    BindingDBiQ08210.
    ChEMBLiCHEMBL3588732.
    DrugBankiDB01117. Atovaquone.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblProtistsiCAG25203; CAG25203; PF3D7_0603300.
    GeneDBiPF3D7_0603300.1:pep.
    GeneIDi3885966.
    KEGGipfa:PFF0160c.

    Organism-specific databases

    EuPathDBiPlasmoDB:PF3D7_0603300.

    Phylogenomic databases

    HOGENOMiHOG000225103.
    InParanoidiQ08210.
    KOiK00254.
    OMAiLMPLGRT.
    PhylomeDBiQ08210.

    Enzyme and pathway databases

    UniPathwayiUPA00070; UER00946.
    ReactomeiR-PFA-500753. Pyrimidine biosynthesis.

    Miscellaneous databases

    EvolutionaryTraceiQ08210.

    Family and domain databases

    CDDicd04738. DHOD_2_like. 1 hit.
    Gene3Di3.20.20.70. 2 hits.
    InterProiIPR013785. Aldolase_TIM.
    IPR005720. Dihydroorotate_DH.
    IPR005719. Dihydroorotate_DH_2.
    IPR001295. Dihydroorotate_DH_CS.
    [Graphical view]
    PfamiPF01180. DHO_dh. 1 hit.
    [Graphical view]
    PROSITEiPS00911. DHODEHASE_1. 1 hit.
    PS00912. DHODEHASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPYRD_PLAF7
    AccessioniPrimary (citable) accession number: Q08210
    Secondary accession number(s): Q6LFN3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: November 30, 2016
    This is version 124 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.