Reviewed, UniProtKB/Swiss-Prot Q874I4 (PYRD_CANAL)

Names and origin

Protein names

Recommended name:
    Dihydroorotate dehydrogenase, mitochondrial
      Short name=DHOdehase
      Short name=DHODase
      Short name=DHOD
    EC=1.3.3.1
Alternative name(s):
    Dihydroorotate oxidase

Gene names

Name:	URA9
Synonyms:	URA1
ORF Names:	CaO19.4836, CaO19.12299

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + O2 = orotate + H2O2.
Cofactor	Binds 1 FAD per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6.
Subcellular location	Mitochondrion inner membrane By similarity.
Sequence similarities	Belongs to the dihydroorotate dehydrogenase family.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dihydroorotate oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 444		Dihydroorotate dehydrogenase, mitochondrial		PRO_0000029891
Sites
	Active site	257	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q874I4-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: CD37C62FFA2E6902	FASTA	444	48,426
	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

References

	« Hide 'large scale' referencesShow '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., Moller K., Loffler M., Piskur J. Mol. Genet. Genomics 271:387-393(2004) [PubMed: 15014982] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Candida albicans DHOD." Hall C.R., Dietrich F.S. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY230865 Genomic DNA. Translation: AAO74621.1. AY240959 Genomic DNA. Translation: AAP39962.1. AACQ01000002 Genomic DNA. Translation: EAL04628.1. AACQ01000001 Genomic DNA. Translation: EAL04824.1.
RefSeq	XP_723332.1. XP_723522.1.
3D structure databases
HSSP	HSSP built from PDB template 1D3G based on UniProtKB Q02127.
ModBase	Search...
Genome annotation databases
GeneID	3634819. 3634949.
Organism-specific databases
CGD	CAL0005359. URA1.
Phylogenomic databases
OMA	Q874I4. AALNRMG.
Enzyme and pathway databases
BRENDA	1.3.3.1. 1124. 1.3.99.11. 1124.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR012135. Dihydroorotate_DH_1_2. IPR005719. Dihydroorotate_DH_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF01180. DHO_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR01036. pyrD_sub2. 1 hit.
PROSITE	PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRD_CANAL

Accession

Primary (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:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)