Reviewed, UniProtKB/Swiss-Prot Q6SZS5 (PYRD_CANGA)

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
Ordered Locus Names:	CAGL0M12881g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

Protein attributes

Sequence length	439 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
Technical term	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 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	? – 439		Dihydroorotate dehydrogenase, mitochondrial		PRO_0000029892
Sites
	Active site	248	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6SZS5-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: E116514C9B8CCBB4	FASTA	439	48,217
	10 20 30 40 50 60 MMHRVGFNVI GRRSFFTVNA RRQVLKSSFM GLKPLQLTAL LLAGSAGYLY FMNARSAIHE 70 80 90 100 110 120 YVVCPVVRLI TPDPENGHKL GIWCFKWGLS PKLYFDKDPE SLHVNVFGTT MTNPIGCAAG 130 140 150 160 170 180 LDKDAEAIDG IMPTGFGYME VGSVTPVAQP GNPRPRFFRL PADDAVINRY GFNSSGHDVV 190 200 210 220 230 240 YNNLMKRVNK FLNSYFGDKS IDKLSLYKDK LLAVNLGKNK NGDEVKDYLK GVEKFQSLAD 250 260 270 280 290 300 VLVINVSSPN TPGLRDLQNE AKLTNLLSEI ITKRDSQSNK PNALGKQNHK PPVLVKIAPD 310 320 330 340 350 360 LTEPELQSIV EAAKKSKVDG IIVSNTTIQR PNTLKTQDET LRNQVGGLSG KPLKPFALKA 370 380 390 400 410 420 MKAVSKYAKD SDLVLVGCGG ISSGKDAIEF AKAGATFVQL YTSYAYVGPA LIARIKDEVA 430 EELKKEGKTW MEIIGEDNK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Hall C.R., Dietrich F.S. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY444340 Genomic DNA. Translation: AAR17523.1. CR380959 Genomic DNA. Translation: CAG62883.1.
RefSeq	XP_449903.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2891454.
KEGG	cgr:CAGL0M12881g.
Phylogenomic databases
HOGENOM	Q6SZS5.
OMA	Q6SZS5. AALNRMG.
Enzyme and pathway databases
BRENDA	1.3.3.1. 189220.
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]
PIRSF	PIRSF000164. DHO_oxidase. 1 hit.
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_CANGA

Accession

Primary (citable) accession number: Q6SZS5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)