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Protein

Dihydroorotase

Gene

URA4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Protein URA2 (URA2)
  2. Protein URA2 (URA2)
  3. Dihydroorotase (URA4)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi14 – 141Zinc 1; via tele nitrogenBy similarity
Metal bindingi16 – 161Zinc 1; via tele nitrogenBy similarity
Metal bindingi98 – 981Zinc 1; via carbamate groupBy similarity
Metal bindingi98 – 981Zinc 2; via carbamate groupBy similarity
Metal bindingi137 – 1371Zinc 2; via pros nitrogenBy similarity
Metal bindingi180 – 1801Zinc 2; via tele nitrogenBy similarity
Metal bindingi258 – 2581Zinc 1By similarity

GO - Molecular functioni

  • dihydroorotase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: SGD
  • 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  • pyrimidine nucleotide biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YLR420W-MONOMER.
BRENDAi3.5.2.3. 984.
UniPathwayiUPA00070; UER00117.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroorotase (EC:3.5.2.3)
Short name:
DHOase
Gene namesi
Name:URA4
Ordered Locus Names:YLR420W
ORF Names:L9931.1
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR420W.
SGDiS000004412. URA4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 364364DihydroorotasePRO_0000147292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981N6-carboxylysineBy similarity

Proteomic databases

MaxQBiP20051.
PeptideAtlasiP20051.

Expressioni

Inductioni

By N-carbamoyl-L-aspartate.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
JSN1P471351EBI-14380,EBI-9422
PHO13P198811EBI-14380,EBI-35376
TOP2P067861EBI-14380,EBI-19352

Protein-protein interaction databases

BioGridi31679. 41 interactions.
DIPiDIP-5074N.
IntActiP20051. 3 interactions.
MINTiMINT-520000.

Structurei

3D structure databases

ProteinModelPortaliP20051.
SMRiP20051. Positions 12-360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family.Curated

Phylogenomic databases

HOGENOMiHOG000256259.
InParanoidiP20051.
KOiK01465.
OMAiYAEAFEQ.
OrthoDBiEOG7Z0K75.

Family and domain databases

InterProiIPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF59. PTHR11647:SF59. 1 hit.
PIRSFiPIRSF001237. DHOdimr. 1 hit.
SUPFAMiSSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR00856. pyrC_dimer. 1 hit.
PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20051-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQEIDLGLT CDMHVHVREG AMCELVTPKI RDGGVSIAYI MPNLQPPITT
60 70 80 90 100
LDRVIEYKKT LQKLAPKTTF LMSFYLSKDL TPDLIHEAAQ QHAIRGVKCY
110 120 130 140 150
PAGVTTNSAA GVDPNDFSAF YPIFKAMQEE NLVLNLHGEK PSVHDGDKEP
160 170 180 190 200
IHVLNAEEAF LPALKKLHND FPNLKIILEH CTSESAIKTI EDINKNVKKA
210 220 230 240 250
TDVKVAATLT AHHLFLTIDD WAGNPVNFCK PVAKLPNDKK ALVKAAVSGK
260 270 280 290 300
PYFFFGSDSA PHPVQNKANY EGVCAGVYSQ SFAIPYIAQV FEEQNALENL
310 320 330 340 350
KGFVSDFGIS FYEVKDSEVA SSDKAILFKK EQVIPQVISD GKDISIIPFK
360
AGDKLSWSVR WEPR
Length:364
Mass (Da):40,313
Last modified:October 1, 1996 - v2
Checksum:iD92FD56E7568FA7C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 11913NSAAG…NDFSA → IRLLGWIQMTSAH (PubMed:2897615).CuratedAdd
BLAST
Sequence conflicti156 – 1561A → R in CAA30444 (PubMed:2897615).Curated
Sequence conflicti240 – 2401K → R in CAA30444 (PubMed:2897615).Curated
Sequence conflicti269 – 2691N → K in CAA30444 (PubMed:2897615).Curated
Sequence conflicti319 – 3191V → M in CAA30444 (PubMed:2897615).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07561 Genomic DNA. Translation: CAA30444.1.
U20162 Genomic DNA. Translation: AAB67491.1.
U20939 Genomic DNA. Translation: AAB67510.1.
BK006945 Genomic DNA. Translation: DAA09722.1.
PIRiS59385. DEBYO.
RefSeqiNP_013524.1. NM_001182308.1.

Genome annotation databases

EnsemblFungiiYLR420W; YLR420W; YLR420W.
GeneIDi851139.
KEGGisce:YLR420W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07561 Genomic DNA. Translation: CAA30444.1.
U20162 Genomic DNA. Translation: AAB67491.1.
U20939 Genomic DNA. Translation: AAB67510.1.
BK006945 Genomic DNA. Translation: DAA09722.1.
PIRiS59385. DEBYO.
RefSeqiNP_013524.1. NM_001182308.1.

3D structure databases

ProteinModelPortaliP20051.
SMRiP20051. Positions 12-360.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31679. 41 interactions.
DIPiDIP-5074N.
IntActiP20051. 3 interactions.
MINTiMINT-520000.

Proteomic databases

MaxQBiP20051.
PeptideAtlasiP20051.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR420W; YLR420W; YLR420W.
GeneIDi851139.
KEGGisce:YLR420W.

Organism-specific databases

EuPathDBiFungiDB:YLR420W.
SGDiS000004412. URA4.

Phylogenomic databases

HOGENOMiHOG000256259.
InParanoidiP20051.
KOiK01465.
OMAiYAEAFEQ.
OrthoDBiEOG7Z0K75.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00117.
BioCyciYEAST:YLR420W-MONOMER.
BRENDAi3.5.2.3. 984.

Miscellaneous databases

NextBioi967895.
PROiP20051.

Family and domain databases

InterProiIPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
IPR032466. Metal_Hydrolase.
[Graphical view]
PANTHERiPTHR11647:SF59. PTHR11647:SF59. 1 hit.
PIRSFiPIRSF001237. DHOdimr. 1 hit.
SUPFAMiSSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR00856. pyrC_dimer. 1 hit.
PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPYRC_YEAST
AccessioniPrimary (citable) accession number: P20051
Secondary accession number(s): D6VZ56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 12700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.