P20051 (PYRC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroorotase
Short name=DHOase
EC=3.5.2.3

Gene names

Name:	URA4
Ordered Locus Names:	YLR420W
ORF Names:	L9931.1

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Induction	By N-carbamoyl-L-aspartate.
Miscellaneous	Present with 12700 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the DHOase family.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from mutant phenotype. Source: SGD pyrimidine nucleotide biosynthetic process Inferred from mutant phenotype Ref.1. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	dihydroorotase activity Inferred from mutant phenotype Ref.1. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
JSN1	P47135	1	EBI-14380,EBI-9422
PHO13	P19881	1	EBI-14380,EBI-35376
TOP2	P06786	1	EBI-14380,EBI-19352

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 364	364	Dihydroorotase		PRO_0000147292
Sites
	Metal binding	14	1	Zinc 1 By similarity
	Metal binding	16	1	Zinc 1 By similarity
	Metal binding	98	1	Zinc 1; via carbamate group By similarity
	Metal binding	98	1	Zinc 2; via carbamate group By similarity
	Metal binding	137	1	Zinc 2 By similarity
	Metal binding	180	1	Zinc 2 By similarity
	Metal binding	258	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	98	1	N6-carboxylysine By similarity
Experimental info
	Sequence conflict	107 – 119	13	NSAAG…NDFSA → IRLLGWIQMTSAH Ref.1
	Sequence conflict	156	1	A → R in CAA30444. Ref.1
	Sequence conflict	240	1	K → R in CAA30444. Ref.1
	Sequence conflict	269	1	N → K in CAA30444. Ref.1
	Sequence conflict	319	1	V → M in CAA30444. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P20051 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: D92FD56E7568FA7C	FASTA	364	40,313
	10 20 30 40 50 60 MVQEIDLGLT CDMHVHVREG AMCELVTPKI RDGGVSIAYI MPNLQPPITT LDRVIEYKKT 70 80 90 100 110 120 LQKLAPKTTF LMSFYLSKDL TPDLIHEAAQ QHAIRGVKCY PAGVTTNSAA GVDPNDFSAF 130 140 150 160 170 180 YPIFKAMQEE NLVLNLHGEK PSVHDGDKEP IHVLNAEEAF LPALKKLHND FPNLKIILEH 190 200 210 220 230 240 CTSESAIKTI EDINKNVKKA TDVKVAATLT AHHLFLTIDD WAGNPVNFCK PVAKLPNDKK 250 260 270 280 290 300 ALVKAAVSGK PYFFFGSDSA PHPVQNKANY EGVCAGVYSQ SFAIPYIAQV FEEQNALENL 310 320 330 340 350 360 KGFVSDFGIS FYEVKDSEVA SSDKAILFKK EQVIPQVISD GKDISIIPFK AGDKLSWSVR WEPR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the Saccharomyces cerevisiae URA4 gene encoding dihydroorotase." Guyonvarch A., Nguyen-Juilleret M., Hubert J.-C., Lacroute F. Mol. Gen. Genet. 212:134-141(1988) [PubMed: 2897615] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 28383 / FL100 / VTT C-80102.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X07561 Genomic DNA. Translation: CAA30444.1. U20162 Genomic DNA. Translation: AAB67491.1. U20939 Genomic DNA. Translation: AAB67510.1. BK006945 Genomic DNA. Translation: DAA09722.1.
PIR	DEBYO. S59385.
RefSeq	NP_013524.1. NM_001182308.1.
3D structure databases
ProteinModelPortal	P20051.
SMR	P20051. Positions 2-361.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5074N.
IntAct	P20051. 3 interactions.
MINT	MINT-520000.
STRING	P20051.
Proteomic databases
PeptideAtlas	P20051.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR420W; YLR420W; YLR420W.
GeneID	851139.
KEGG	sce:YLR420W.
NMPDR	fig|4932.3.peg.4554.
Organism-specific databases
CYGD	YLR420w.
SGD	S000004412. URA4.
Phylogenomic databases
eggNOG	fuNOG04770.
GeneTree	EFGT00050000006781.
HOGENOM	HBG628648.
OMA	CLPVAKR.
OrthoDB	EOG4HTD20.
Enzyme and pathway databases
BRENDA	3.5.2.3. 984.
Gene expression databases
ArrayExpress	P20051.
Genevestigator	P20051.
GermOnline	YLR420W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004721. DHOdimr. IPR002195. Dihydroorotase_CS. [Graphical view]
KO	K01465.
PIRSF	PIRSF001237. DHOdimr. 1 hit.
TIGRFAMs	TIGR00856. PyrC_dimer. 1 hit.
PROSITE	PS00482. DIHYDROOROTASE_1. 1 hit. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967895.

Entry information

Entry name

PYRC_YEAST

Accession

Primary (citable) accession number: P20051
Secondary accession number(s): D6VZ56

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program