Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydroorotate dehydrogenase (fumarate)

Gene

pyr4

Organism
Trypanosoma cruzi (strain CL Brener)
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=57.3 µM for dihydroorotate1 Publication
  2. KM=62.2 µM for fumarate1 Publication

    pH dependencei

    Optimum pH is 7.1 Publication

    Temperature dependencei

    Optimum temperature is 37 degrees Celsius.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 sitei21 – 211FMN; via carbonyl oxygen1 Publication
    Binding sitei45 – 451Substrate
    Binding sitei129 – 1291FMN1 Publication
    Binding sitei129 – 1291Substrate
    Active sitei132 – 1321NucleophileBy similarity
    Binding sitei134 – 1341Substrate
    Binding sitei166 – 1661FMN1 Publication
    Binding sitei195 – 1951FMN; via carbonyl oxygen1 Publication
    Binding sitei224 – 2241FMN; via amide nitrogen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi45 – 462FMN1 Publication
    Nucleotide bindingi251 – 2522FMN1 Publication
    Nucleotide bindingi273 – 2742FMN1 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

    BioCyciMetaCyc:MONOMER-14470.
    BRENDAi1.3.5.2. 6524.
    1.3.98.1. 6524.
    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
    Name:pyr4
    Synonyms:tcdhod2
    ORF Names:Tc00.1047053508375.50
    OrganismiTrypanosoma cruzi (strain CL Brener)
    Taxonomic identifieri353153 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum
    Proteomesi
    • UP000002296 Componenti: Unassembled WGS sequence

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 314314Dihydroorotate dehydrogenase (fumarate)PRO_0000409558Add
    BLAST

    Proteomic databases

    PaxDbiQ4D3W2.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi353153.XP_809064.1.

    Structurei

    Secondary structure

    1
    314
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 83Combined sources
    Beta strandi11 – 199Combined sources
    Helixi28 – 369Combined sources
    Beta strandi40 – 434Combined sources
    Beta strandi60 – 634Combined sources
    Beta strandi66 – 694Combined sources
    Helixi78 – 8710Combined sources
    Turni91 – 933Combined sources
    Beta strandi96 – 1005Combined sources
    Helixi105 – 12218Combined sources
    Beta strandi125 – 1295Combined sources
    Helixi141 – 1433Combined sources
    Helixi145 – 15915Combined sources
    Beta strandi163 – 1675Combined sources
    Helixi173 – 18412Combined sources
    Beta strandi189 – 1946Combined sources
    Beta strandi198 – 2025Combined sources
    Turni206 – 2094Combined sources
    Beta strandi210 – 2123Combined sources
    Helixi215 – 2184Combined sources
    Beta strandi219 – 2246Combined sources
    Helixi225 – 2273Combined sources
    Helixi228 – 24114Combined sources
    Beta strandi245 – 2528Combined sources
    Helixi256 – 26510Combined sources
    Beta strandi268 – 2725Combined sources
    Helixi274 – 2796Combined sources
    Helixi283 – 29816Combined sources
    Turni304 – 3085Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DJLX-ray1.38A/B1-314[»]
    2DJXX-ray1.58A/B1-314[»]
    2E68X-ray1.38A/B1-314[»]
    2E6AX-ray1.64A/B1-314[»]
    2E6DX-ray1.94A/B1-314[»]
    2E6FX-ray1.26A/B1-314[»]
    3C3NX-ray2.20A/B/C/D3-314[»]
    3W1AX-ray1.42A/B2-314[»]
    3W1LX-ray1.70A/B2-314[»]
    3W1MX-ray1.90A/B2-314[»]
    3W1NX-ray2.40A/B2-314[»]
    3W1PX-ray2.00A/B2-314[»]
    3W1QX-ray1.85A/B2-314[»]
    3W1RX-ray1.58A/B2-314[»]
    3W1TX-ray1.68A/B2-314[»]
    3W1UX-ray1.85A/B2-314[»]
    3W1XX-ray1.45A/B2-314[»]
    3W22X-ray1.98A/B2-314[»]
    3W23X-ray1.48A/B2-314[»]
    3W2JX-ray1.42A/B2-314[»]
    3W2KX-ray1.54A/B2-314[»]
    3W2LX-ray1.64A/B2-314[»]
    3W2MX-ray1.58A/B2-314[»]
    3W2NX-ray1.96A/B2-314[»]
    3W2UX-ray2.25A/B2-314[»]
    3W3OX-ray1.96A/B2-314[»]
    3W6YX-ray2.68A/B2-314[»]
    3W70X-ray2.60A/B2-314[»]
    3W71X-ray1.68A/B2-314[»]
    3W72X-ray1.55A/B2-314[»]
    3W73X-ray1.78A/B2-314[»]
    3W74X-ray1.90A/B2-314[»]
    3W75X-ray1.47A/B2-314[»]
    3W76X-ray1.58A/B2-314[»]
    3W7CX-ray1.75A/B2-314[»]
    3W7DX-ray1.52A/B2-314[»]
    3W7EX-ray1.56A/B2-314[»]
    3W7GX-ray1.55A/B2-314[»]
    3W7HX-ray1.67A/B2-314[»]
    3W7IX-ray1.69A/B2-314[»]
    3W7JX-ray1.58A/B2-314[»]
    3W7KX-ray1.61A/B2-314[»]
    3W7LX-ray1.88A/B2-314[»]
    3W7MX-ray2.40A/B2-314[»]
    3W7NX-ray2.39A/B2-314[»]
    3W7OX-ray1.68A/B2-314[»]
    3W7PX-ray1.70A/B2-314[»]
    3W7QX-ray1.83A/B2-314[»]
    3W83X-ray2.80A/B2-314[»]
    3W84X-ray1.93A/B2-314[»]
    3W85X-ray2.00A/B2-314[»]
    3W86X-ray1.50A/B2-314[»]
    3W87X-ray1.43A/B2-314[»]
    3W88X-ray1.40A/B2-314[»]
    4JD4X-ray1.51A/B2-314[»]
    4JDBX-ray1.82A/B2-314[»]
    ProteinModelPortaliQ4D3W2.
    SMRiQ4D3W2. Positions 2-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ4D3W2.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni69 – 735Substrate binding
    Regioni196 – 1972Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1436. Eukaryota.
    COG0167. LUCA.
    KOiK00226.

    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.

    Q4D3W2-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MMCLKLNLLD HVFANPFMNA AGVLCSTEED LRCMTASSSG ALVSKSCTSA
    60 70 80 90 100
    PRDGNPEPRY MAFPLGSINS MGLPNLGFDF YLKYASDLHD YSKKPLFLSI
    110 120 130 140 150
    SGLSVEENVA MVRRLAPVAQ EKGVLLELNL SCPNVPGKPQ VAYDFEAMRT
    160 170 180 190 200
    YLQQVSLAYG LPFGVKMPPY FDIAHFDTAA AVLNEFPLVK FVTCVNSVGN
    210 220 230 240 250
    GLVIDAESES VVIKPKQGFG GLGGKYILPT ALANVNAFYR RCPDKLVFGC
    260 270 280 290 300
    GGVYSGEDAF LHILAGASMV QVGTALQEEG PGIFTRLEDE LLEIMARKGY
    310
    RTLEEFRGRV KTIE
    Length:314
    Mass (Da):34,167
    Last modified:September 13, 2005 - v1
    Checksum:i86917A54E3CD11FD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1211E → G in BAA74526 (PubMed:16020725).Curated
    Sequence conflicti121 – 1211E → G in BAA31360 (PubMed:16020725).Curated
    Sequence conflicti141 – 1411V → G in BAA74526 (PubMed:16020725).Curated
    Sequence conflicti141 – 1411V → G in BAA31360 (PubMed:16020725).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21M → T in allele DHOD3.
    Natural varianti3 – 31C → R in alleles DHOD2 and DHOD3.
    Natural varianti63 – 631F → V in allele DHOD2.
    Natural varianti86 – 861S → I in alleles DHOD2 and DHOD3.
    Natural varianti98 – 981L → V in allele DHOD3.
    Natural varianti222 – 2221L → I in alleles DHOD2 and DHOD3.
    Natural varianti285 – 2851T → R in allele DHOD3.
    Natural varianti301 – 3011R → K in allele DHOD2.

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAHK01001070 Genomic DNA. Translation: EAN87213.1.
    AB010286 Genomic DNA. Translation: BAA31360.1.
    AB017765 Genomic DNA. Translation: BAA74526.1.
    AB212956 Genomic DNA. Translation: BAE48283.1.
    PIRiT30523.
    RefSeqiXP_809064.1. XM_803971.1.

    Genome annotation databases

    EnsemblProtistsiEAN87213; EAN87213; Tc00.1047053508375.50.
    GeneIDi3539620.
    KEGGitcr:508375.50.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAHK01001070 Genomic DNA. Translation: EAN87213.1.
    AB010286 Genomic DNA. Translation: BAA31360.1.
    AB017765 Genomic DNA. Translation: BAA74526.1.
    AB212956 Genomic DNA. Translation: BAE48283.1.
    PIRiT30523.
    RefSeqiXP_809064.1. XM_803971.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DJLX-ray1.38A/B1-314[»]
    2DJXX-ray1.58A/B1-314[»]
    2E68X-ray1.38A/B1-314[»]
    2E6AX-ray1.64A/B1-314[»]
    2E6DX-ray1.94A/B1-314[»]
    2E6FX-ray1.26A/B1-314[»]
    3C3NX-ray2.20A/B/C/D3-314[»]
    3W1AX-ray1.42A/B2-314[»]
    3W1LX-ray1.70A/B2-314[»]
    3W1MX-ray1.90A/B2-314[»]
    3W1NX-ray2.40A/B2-314[»]
    3W1PX-ray2.00A/B2-314[»]
    3W1QX-ray1.85A/B2-314[»]
    3W1RX-ray1.58A/B2-314[»]
    3W1TX-ray1.68A/B2-314[»]
    3W1UX-ray1.85A/B2-314[»]
    3W1XX-ray1.45A/B2-314[»]
    3W22X-ray1.98A/B2-314[»]
    3W23X-ray1.48A/B2-314[»]
    3W2JX-ray1.42A/B2-314[»]
    3W2KX-ray1.54A/B2-314[»]
    3W2LX-ray1.64A/B2-314[»]
    3W2MX-ray1.58A/B2-314[»]
    3W2NX-ray1.96A/B2-314[»]
    3W2UX-ray2.25A/B2-314[»]
    3W3OX-ray1.96A/B2-314[»]
    3W6YX-ray2.68A/B2-314[»]
    3W70X-ray2.60A/B2-314[»]
    3W71X-ray1.68A/B2-314[»]
    3W72X-ray1.55A/B2-314[»]
    3W73X-ray1.78A/B2-314[»]
    3W74X-ray1.90A/B2-314[»]
    3W75X-ray1.47A/B2-314[»]
    3W76X-ray1.58A/B2-314[»]
    3W7CX-ray1.75A/B2-314[»]
    3W7DX-ray1.52A/B2-314[»]
    3W7EX-ray1.56A/B2-314[»]
    3W7GX-ray1.55A/B2-314[»]
    3W7HX-ray1.67A/B2-314[»]
    3W7IX-ray1.69A/B2-314[»]
    3W7JX-ray1.58A/B2-314[»]
    3W7KX-ray1.61A/B2-314[»]
    3W7LX-ray1.88A/B2-314[»]
    3W7MX-ray2.40A/B2-314[»]
    3W7NX-ray2.39A/B2-314[»]
    3W7OX-ray1.68A/B2-314[»]
    3W7PX-ray1.70A/B2-314[»]
    3W7QX-ray1.83A/B2-314[»]
    3W83X-ray2.80A/B2-314[»]
    3W84X-ray1.93A/B2-314[»]
    3W85X-ray2.00A/B2-314[»]
    3W86X-ray1.50A/B2-314[»]
    3W87X-ray1.43A/B2-314[»]
    3W88X-ray1.40A/B2-314[»]
    4JD4X-ray1.51A/B2-314[»]
    4JDBX-ray1.82A/B2-314[»]
    ProteinModelPortaliQ4D3W2.
    SMRiQ4D3W2. Positions 2-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi353153.XP_809064.1.

    Proteomic databases

    PaxDbiQ4D3W2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblProtistsiEAN87213; EAN87213; Tc00.1047053508375.50.
    GeneIDi3539620.
    KEGGitcr:508375.50.

    Phylogenomic databases

    eggNOGiKOG1436. Eukaryota.
    COG0167. LUCA.
    KOiK00226.

    Enzyme and pathway databases

    UniPathwayiUPA00070.
    BioCyciMetaCyc:MONOMER-14470.
    BRENDAi1.3.5.2. 6524.
    1.3.98.1. 6524.

    Miscellaneous databases

    EvolutionaryTraceiQ4D3W2.

    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...

    Entry informationi

    Entry nameiPYRD_TRYCC
    AccessioniPrimary (citable) accession number: Q4D3W2
    Secondary accession number(s): O76140
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 31, 2011
    Last sequence update: September 13, 2005
    Last modified: November 11, 2015
    This is version 79 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.