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Q57U83 (PYRD_TRYB2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase (fumarate)
Short name=DHOD
Short name=DHODase
Short name=DHOdehase
EC=1.3.98.1
Alternative name(s):
Dihydroorotate oxidase
Gene names
ORF Names:Tb927.5.3830
OrganismTrypanosoma brucei brucei (strain 927/4 GUTat10.1) [Complete proteome]
Taxonomic identifier999953 [NCBI]
Taxonomic lineageEukaryota › Euglenozoa › Kinetoplastida › Trypanosomatidae › Trypanosoma

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 FMN per subunit. Ref.2

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway.

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=14 µM for dihydroorotate Ref.2

KM=80 µM for fumarate

pH dependence:

Optimum pH is 7.8.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological process'de novo' pyrimidine base biosynthetic process

Inferred from electronic annotation. Source: InterPro

UMP biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Dihydroorotate dehydrogenase (fumarate)
PRO_0000409559

Regions

Nucleotide binding44 – 452FMN
Nucleotide binding249 – 2513FMN
Nucleotide binding272 – 2732FMN
Region68 – 725Substrate binding
Region195 – 1962Substrate binding

Sites

Active site1311Nucleophile By similarity
Binding site201FMN; via carbonyl oxygen
Binding site441Substrate
Binding site1281FMN
Binding site1281Substrate
Binding site1331Substrate
Binding site1651FMN
Binding site1941FMN; via carbonyl oxygen
Binding site2231FMN; via amide nitrogen
Binding site2491FMN

Secondary structure

1 ........................................ 313
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q57U83 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: C005E7470D4C1EA1

FASTA31334,112
        10         20         30         40         50         60 
MSLKVNILGH EFSNPFMNAA GVLCTTEEDL RRMTESESGS LIGKSCTLAP RTGNPEPRYF 

        70         80         90        100        110        120 
GLPLGSINSM GLPNLGVDFY LSYAAQTHDY SRKPLFLSMS GLSVEESVEM VKKLAPITKE 

       130        140        150        160        170        180 
KGTILELNLS CPNVPGKPQV GYDFDTTRTY LQKVSEAYGL PFGVKMPPYF DIAHFDMAAA 

       190        200        210        220        230        240 
VLNDFPLVKF ITCVNSIGNG LVIDPANETV VIKPKQGFGG LGGKYVLPTA LANVNAFFRR 

       250        260        270        280        290        300 
CPDKLVFGCG GVYSGEEAFL HILAGASMVQ VGTALHDEGP IIFARLNKEL QEIMTNKGYK 

       310 
TLDEFRGRVK TMD

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 16020726] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 927/4 GUTat10.1.
[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: 18312275] [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC159455 Genomic DNA. Translation: AAX70836.1.
CP000068 Genomic DNA. Translation: AAZ11494.1.
RefSeqXP_845053.1. XM_839960.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B4GX-ray1.95A/B/C/D1-313[»]
ProteinModelPortalQ57U83.
SMRQ57U83. Positions 1-313.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ57U83.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsAAZ11494; AAZ11494; Tb927.5.3830.
GeneID3657493.

Organism-specific databases

EuPathDBEupathDB:Tb927.5.3830.

Phylogenomic databases

HOGENOMHBG472415.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR012135. Dihydroorotate_DH_1_2.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01037. PyrD_sub1_fam. 1 hit.
PROSITEPS00911. DHODEHASE_1. False negative.
PS00912. DHODEHASE_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_TRYB2
AccessionPrimary (citable) accession number: Q57U83
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: May 10, 2005
Last modified: January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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