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Q874I4 (PYRD_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. 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 (quinone), mitochondrial
Short name=DHOD
Short name=DHODase
Short name=DHOdehase
EC=1.3.5.2
Alternative name(s):
Dihydroorotate oxidase
Gene names
Name:URA9
Synonyms:URA1
ORF Names:CaO19.4836, CaO19.12299
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In the de novo pyrimidine biosynthesic pathway, catalyzes the stereospecific oxidation of (S)-dihydroorotate to orotate with reduction of flavin and the transfer of electrons to ubiquinone, which is part of the repiratory chain. Does not use fumarate and NAD as electron acceptors. Ref.4

Catalytic activity

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

Cofactor

Binds 1 FMN per subunit By similarity. Ref.4

Enzyme regulation

Inhibited by the dianisidine derivative redoxal and by brequinar.

Pathway

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

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=108 µM for (S)-dihydroorotate Ref.4

KM=42 µM for decylubiquinone

KM=122 µM for 2,6-dichloroindophenol

Vmax=6 µmol/min/mg enzyme

pH dependence:

Optimum pH is 8.0-8.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion Potential
Chain28 – 444417Dihydroorotate dehydrogenase (quinone), mitochondrial
PRO_0000029891

Regions

Transmembrane33 – 5321Helical; Potential
Nucleotide binding124 – 1285FMN By similarity
Nucleotide binding406 – 4072FMN By similarity
Region173 – 1775Substrate binding By similarity
Region254 – 2596Substrate binding By similarity
Region329 – 3302Substrate binding By similarity

Sites

Active site2571Nucleophile By similarity
Binding site1281Substrate By similarity
Binding site1481FMN By similarity
Binding site2241FMN By similarity
Binding site2541FMN By similarity
Binding site3001FMN By similarity
Binding site3281FMN; via carbonyl oxygen By similarity
Binding site3551FMN; via amide nitrogen By similarity
Binding site3851FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q874I4 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: CD37C62FFA2E6902

FASTA44448,426
        10         20         30         40         50         60 
MFRPSIKFKQ STLSIIARRL KSSAQHQPLR SSFVPSPIVF VAGLAVAAVG GYYCLDSRSA 

        70         80         90        100        110        120 
IHEYVLCPLI RTFTDAESGH KLGIFFMKYG LSPRLLDDGK NDQSDVLGVQ VFGHKLKNPI 

       130        140        150        160        170        180 
GLAAGLDKDG EAIESLFNCG FSYVEIGSIT PEPQPGNPQP RFFRLPKDDA VINRYGFNSS 

       190        200        210        220        230        240 
GHFNVLATLK LRFNKLLNKF GTSHSSEQHP FSNAFQQGKL LGINLGKNKF GDEVNDYVKG 

       250        260        270        280        290        300 
VERLGPYADV LVINVSSPNT PGLRDLQSEA KLTNLLTTVV KERNVLGKNL LGNKPPVLVK 

       310        320        330        340        350        360 
VAPDLTEPEI ESIANSAKEA KVDGIIISNT TIQRPVDRLL TTDKQLINQA GGLSGKPLKP 

       370        380        390        400        410        420 
LSLKALRTLR KYTKDSDLVL IGCGGISNGK DALEFGKAGA TFIELYTAFA YKGPGLVGKI 

       430        440 
RDELAEELRK EGKTWEQIIG SDDK

« Hide

References

« Hide 'large scale' references
[1]"Horizontal gene transfer promoted evolution of the ability to propagate under anaerobic conditions in yeasts."
Gojkovic Z., Knecht W., Zameitat E., Warneboldt J., Coutelis J.-B., Pynyaha Y., Neuveglise C., Moeller K., Loeffler M., Piskur J.
Mol. Genet. Genomics 271:387-393(2004) [PubMed: 15014982] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Contribution of horizontal gene transfer to the evolution of Saccharomyces cerevisiae."
Hall C.R., Brachat S., Dietrich F.S.
Eukaryot. Cell 4:1102-1115(2005) [PubMed: 15947202] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MMRL 2010.
[3]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.
[4]"Biochemical characterization of recombinant dihydroorotate dehydrogenase from the opportunistic pathogenic yeast Candida albicans."
Zameitat E., Gojkovic Z., Knecht W., Piskur J., Loeffler M.
FEBS J. 273:3183-3191(2006) [PubMed: 16774642] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY230865 Genomic DNA. Translation: AAO74621.1.
AY240959 Genomic DNA. Translation: AAP39962.1.
AACQ01000002 Genomic DNA. Translation: EAL04628.1.
AACQ01000001 Genomic DNA. Translation: EAL04824.1.
RefSeqXP_723332.1. XM_718239.1.
XP_723522.1. XM_718429.1.

3D structure databases

ProteinModelPortalQ874I4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ874I4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3634819.
3634949.
KEGGcal:CaO19.12299.
cal:CaO19.4836.

Organism-specific databases

CGDCAL0005359. URA1.

Phylogenomic databases

OMAAALNRMG.
PhylomeDBQ874I4.

Enzyme and pathway databases

BRENDA1.3.99.11. 1096.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00226.
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR01036. PyrD_sub2. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_CANAL
AccessionPrimary (citable) accession number: Q874I4
Secondary accession number(s): Q5APC9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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