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Q08210 (PYRD_PLAF7) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase (quinone), mitochondrial
Short name=DHOdehase
EC=1.3.5.2
Alternative name(s):
Dihydroorotate oxidase
Gene names
ORF Names:PFF0160c
OrganismPlasmodium falciparum (isolate 3D7)
Taxonomic identifier36329 [NCBI]
Taxonomic lineageEukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania)

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 FMN per subunit. Ref.4 Ref.5 Ref.6

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion inner membrane By similarity; Single-pass membrane protein Potential.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Biophysicochemical properties

Kinetic parameters:

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2323Mitochondrion Potential
Chain24 – 569546Dihydroorotate dehydrogenase (quinone), mitochondrial
PRO_0000029888

Regions

Transmembrane143 – 16321Helical; Potential
Nucleotide binding225 – 2295FMN
Nucleotide binding477 – 4782FMN
Nucleotide binding505 – 5073FMN
Nucleotide binding528 – 5292FMN
Region274 – 2785Substrate binding
Region458 – 4592Substrate binding

Sites

Active site3451Nucleophile By similarity
Binding site2291Substrate
Binding site2491FMN
Binding site3421FMN
Binding site3421Substrate
Binding site3471Substrate
Binding site4291FMN

Secondary structure

1 ................................................................. 569
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08210 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 88880384EBD52FE3

FASTA56965,558
        10         20         30         40         50         60 
MISKLKPQFM FLPKKHILSY CRKDVLNLFE QKFYYTSKRK ESNNMKNESL LRLINYNRYY 

        70         80         90        100        110        120 
NKIDSNNYYN GGKILSNDRQ YIYSPLCEYK KKINDISSYV SVPFKINIRN LGTSNFVNNK 

       130        140        150        160        170        180 
KDVLDNDYIY ENIKKEKSKH KKIIFLLFVS LFGLYGFFES YNPEFFLYDI FLKFCLKYID 

       190        200        210        220        230        240 
GEICHDLFLL LGKYNILPYD TSNDSIYACT NIKHLDFINP FGVAAGFDKN GVCIDSILKL 

       250        260        270        280        290        300 
GFSFIEIGTI TPRGQTGNAK PRIFRDVESR SIINSCGFNN MGCDKVTENL ILFRKRQEED 

       310        320        330        340        350        360 
KLLSKHIVGV SIGKNKDTVN IVDDLKYCIN KIGRYADYIA INVSSPNTPG LRDNQEAGKL 

       370        380        390        400        410        420 
KNIILSVKEE IDNLEKNNIM NDESTYNEDN KIVEKKNNFN KNNSHMMKDA KDNFLWFNTT 

       430        440        450        460        470        480 
KKKPLVFVKL APDLNQEQKK EIADVLLETN IDGMIISNTT TQINDIKSFE NKKGGVSGAK 

       490        500        510        520        530        540 
LKDISTKFIC EMYNYTNKQI PIIASGGIFS GLDALEKIEA GASVCQLYSC LVFNGMKSAV 

       550        560 
QIKRELNHLL YQRGYYNLKE AIGRKHSKS

« Hide

References

« Hide 'large scale' references
[1]"The dihydroorotate dehydrogenase gene homologue of Plasmodium falciparum."
Leblanc S.B., Wilson C.M.
Mol. Biochem. Parasitol. 60:349-352(1993) [PubMed: 8232427] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genome sequence of the human malaria parasite Plasmodium falciparum."
Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D., Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S. expand/collapse author list , Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M., Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A., Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I., Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J., Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.
Nature 419:498-511(2002) [PubMed: 12368864] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Isolate 3D7.
[3]"Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13."
Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D., Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K., Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T., Christodoulou Z. expand/collapse author list , Clark L., Clark R., Corton C., Cronin A., Davies R.M., Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A., Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H., Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D., Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N., Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P., Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A., Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M., Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S., Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R., Sulston J.E., Craig A., Newbold C., Barrell B.G.
Nature 419:527-531(2002) [PubMed: 12368867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Isolate 3D7.
[4]"Structure of Plasmodium falciparum dihydroorotate dehydrogenase with a bound inhibitor."
Hurt D.E., Widom J., Clardy J.
Acta Crystallogr. D 62:312-323(2006) [PubMed: 16510978] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 158-569 IN COMPLEX WITH FMN; OROTATE AND INHIBITOR, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Structural plasticity of malaria dihydroorotate dehydrogenase allows selective binding of diverse chemical scaffolds."
Deng X., Gujjar R., El Mazouni F., Kaminsky W., Malmquist N.A., Goldsmith E.J., Rathod P.K., Phillips M.A.
J. Biol. Chem. 284:26999-27009(2009) [PubMed: 19640844] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 158-569 IN COMPLEXES WITH FMN; OROTATE AND INHIBITORS, COFACTOR.
[6]"Novel inhibitors of Plasmodium falciparum dihydroorotate dehydrogenase with anti-malarial activity in the mouse model."
Booker M.L., Bastos C.M., Kramer M.L., Barker R.H. Jr., Skerlj R., Sidhu A.B., Deng X., Celatka C., Cortese J.F., Guerrero Bravo J.E., Crespo Llado K.N., Serrano A.E., Angulo-Barturen I., Jimenez-Diaz M.B., Viera S., Garuti H., Wittlin S., Papastogiannidis P. expand/collapse author list , Lin J.W., Janse C.J., Khan S.M., Duraisingh M., Coleman B., Goldsmith E.J., Phillips M.A., Munoz B., Wirth D.F., Klinger J.D., Wiegand R., Sybertz E.
J. Biol. Chem. 285:33054-33064(2010) [PubMed: 20702404] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 158-569 IN COMPLEX WITH FMN; OROTATE AND INHIBITOR, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L15446 Unassigned DNA. Translation: AAC37170.1.
AL844505 Genomic DNA. Translation: CAG25203.1.
RefSeqXP_966023.1. XM_960930.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ08210.
SMRQ08210. Positions 158-566.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsPFF0160c:mRNA; PFF0160c:pep; PFF0160c.
GeneID3885966.
KEGGpfa:PFF0160c.
NMPDRfig|36329.1.peg.3381.

Organism-specific databases

EuPathDBEupathDB:PFF0160c.

Phylogenomic databases

GeneTreeEPrGT00060000009676.
ProtClustDBCLSZ2497370.

Enzyme and pathway databases

BRENDA1.3.3.1. 4889.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 2 hits.
KOK00226.
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00359. Sulfadiazine.
DB00664. Sulfametopyrazine.
DB00263. Sulfisoxazole.
DB01145. Sulfoxone.

Entry information

Entry namePYRD_PLAF7
AccessionPrimary (citable) accession number: Q08210
Secondary accession number(s): Q6LFN3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 25, 2012
This is version 85 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents