Reviewed, UniProtKB/Swiss-Prot Q7Z895 (PYD1_KLULA)

Names and origin

Protein names

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

Gene names

Name:	URA1
Ordered Locus Names:	KLLA0C19360g

Organism

Kluyveromyces lactis (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

28985 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	315 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + O(2) = orotate + H(2)O(2).
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	CytoplasmBy similarity.
Miscellaneous	K.lactis has two isoforms of DHODase, a cytoplasmic isoform and a mitochondrial isoform.
Sequence similarities	Belongs to the dihydroorotate dehydrogenase family.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cytoplasm
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	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	dihydroorotate oxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 315	315	Dihydroorotate dehydrogenase		PRO_0000148500
Sites
	Active site	133	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7Z895-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 46DAE6484E4A26A0	FASTA	315	34,989
	10 20 30 40 50 60 MKPSLQVEFC GHIYENPLMN ASGVCCMTTN ELDDMARSSS GAFITKSATS MERDGNPEPR 70 80 90 100 110 120 YVSVPLGSIN SMGLPNKGID YYLDYVLDRQ DRFPSENPPF MSVAGMSIDE NIKLLHRIQD 130 140 150 160 170 180 SNFRGITELN LSCPNVPGKP QVAYDFELTD QILSSVFEFF TKPLGVKLPP YFDFAHFDAM 190 200 210 220 230 240 ACILNKYPIA YVNCINSVGN GLYIDVEKES VVIKPKDGFG GIGGEYIKPT ALANVRAFYN 250 260 270 280 290 300 RLNGRIRIIG TGGIKTGQDA FEHLLCGATM LQIGTELQNE GTEIFERINA ELLQILEQKG 310 YQSIEDFRGK LRSIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Kluyveromyces lactis gene encoding the biosynthetic enzyme dihydroorotate dehydrogenase family 1a." Hall C.R., Dietrich F.S. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 200962 / CBS 141 / HA 714.
[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 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY323896 Genomic DNA. Translation: AAQ01773.1. CR382123 Genomic DNA. Translation: CAH01915.1.
RefSeq	XP_453064.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2891827.
KEGG	kla:KLLA0C19360g.
Phylogenomic databases
HOGENOM	Q7Z895.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR012135. DHO_DHase_1_2. IPR005720. DHO_DHase_1_core. IPR001295. Dihydroorotate_DHase_core. [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	TIGR01037. pyrD_sub1_fam. 1 hit.
PROSITE	PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYD1_KLULA

Accession

Primary (citable) accession number: Q7Z895

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	October 1, 2003
Last modified:	November 25, 2008
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)