Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Dihydroorotate dehydrogenase (fumarate)

Gene

URA1

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

Functioni

Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro. Does not use oxaloacetate or NAD or NADP as electron acceptors.6 Publications

Catalytic activityi

(S)-dihydroorotate + fumarate = orotate + succinate.1 Publication

Cofactori

FMN1 PublicationNote: Binds 1 FMN per subunit.1 Publication

Enzyme regulationi

The activity is independent of the presence of oxygen.

Kineticsi

  1. KM=8.4 µM for (S)-dihydroorotate (at pH 7.5)3 Publications
  2. KM=45 µM for fumarate (at pH 7.5)3 Publications
  3. KM=115 µM for 2,6-dichloroindophenol3 Publications
  1. Vmax=20.4 µmol/min/mg enzyme (with 2,6-dichloroindophenol as electron acceptor)3 Publications
  2. Vmax=5.1 µmol/min/mg enzyme (with fumarate as electron acceptor)3 Publications

pH dependencei

Optimum pH is 8.5. Active from pH 7 to pH 10.3 Publications

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in the pathway UMP biosynthesis via de novo pathway, which is part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei46SubstrateBy similarity1
Binding sitei130FMNBy similarity1
Binding sitei130SubstrateBy similarity1
Active sitei133NucleophileBy similarity1
Binding sitei167FMNBy similarity1
Binding sitei195FMN; via carbonyl oxygenBy similarity1
Binding sitei224FMN; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi46 – 47FMNBy similarity2
Nucleotide bindingi252 – 253FMNBy similarity2
Nucleotide bindingi274 – 275FMNBy similarity2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciMetaCyc:YKL216W-MONOMER.
YEAST:YKL216W-MONOMER.
ReactomeiR-SCE-500753. Pyrimidine biosynthesis.
SABIO-RKP28272.
UniPathwayiUPA00070.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroorotate dehydrogenase (fumarate) (EC:1.3.98.1)
Short name:
DHOD
Short name:
DHODase
Short name:
DHOdehase
Alternative name(s):
Dihydroorotate oxidase
Gene namesi
Name:URA1
Ordered Locus Names:YKL216W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL216W.
SGDiS000001699. URA1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • extrinsic component of membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5621.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001485061 – 314Dihydroorotate dehydrogenase (fumarate)Add BLAST314

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP28272.
PRIDEiP28272.

PTM databases

iPTMnetiP28272.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi33949. 51 interactors.
DIPiDIP-6573N.
IntActiP28272. 2 interactors.
MINTiMINT-709357.

Chemistry databases

BindingDBiP28272.

Structurei

3D structure databases

ProteinModelPortaliP28272.
SMRiP28272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni70 – 74Substrate bindingBy similarity5
Regioni196 – 197Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00500000044924.
HOGENOMiHOG000225104.
InParanoidiP28272.
KOiK00226.
OMAiGGISGKC.
OrthoDBiEOG092C37TJ.

Family and domain databases

CDDicd04741. DHOD_1A_like. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00224. DHO_dh_type1. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR033886. DHOD_1A.
IPR005720. Dihydroorotate_DH.
IPR024920. Dihydroorotate_DH_1.
IPR012135. Dihydroorotate_DH_1_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsiTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEiPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28272-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTASLTTKFL NNTYENPFMN ASGVHCMTTQ ELDELANSKA GAFITKSATT
60 70 80 90 100
LEREGNPEPR YISVPLGSIN SMGLPNEGID YYLSYVLNRQ KNYPDAPAIF
110 120 130 140 150
FSVAGMSIDE NLNLLRKIQD SEFNGITELN LSCPNVPGKP QVAYDFDLTK
160 170 180 190 200
ETLEKVFAFF KKPLGVKLPP YFDFAHFDIM AKILNEFPLA YVNSINSIGN
210 220 230 240 250
GLFIDVEKES VVVKPKNGFG GIGGEYVKPT ALANVRAFYT RLRPEIKVIG
260 270 280 290 300
TGGIKSGKDA FEHLLCGASM LQIGTELQKE GVKIFERIEK ELKDIMEAKG
310
YTSIDQFRGK LNSI
Length:314
Mass (Da):34,801
Last modified:December 1, 1992 - v1
Checksum:i0F1FF9BDA7F8D68E
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti58E → K in strain: CLIB 95, CLIB 219, CLIB 382, CLIB 388, CLIB 413, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83295 Genomic DNA. Translation: AAA34566.1.
X59371 Genomic DNA. Translation: CAA42014.1.
AJ585637 Genomic DNA. Translation: CAE52157.1.
AJ585638 Genomic DNA. Translation: CAE52158.1.
AJ585639 Genomic DNA. Translation: CAE52159.1.
AJ585640 Genomic DNA. Translation: CAE52160.1.
AJ585641 Genomic DNA. Translation: CAE52161.1.
AJ585642 Genomic DNA. Translation: CAE52162.1.
AJ585643 Genomic DNA. Translation: CAE52163.1.
AJ585644 Genomic DNA. Translation: CAE52164.1.
AJ585645 Genomic DNA. Translation: CAE52165.1.
AJ585646 Genomic DNA. Translation: CAE52166.1.
AJ585647 Genomic DNA. Translation: CAE52167.1.
AJ585648 Genomic DNA. Translation: CAE52168.1.
AJ585649 Genomic DNA. Translation: CAE52169.1.
AJ585650 Genomic DNA. Translation: CAE52170.1.
AJ585651 Genomic DNA. Translation: CAE52171.1.
X75951 Genomic DNA. Translation: CAA53557.1.
Z28216 Genomic DNA. Translation: CAA82061.1.
BK006944 Genomic DNA. Translation: DAA08953.1.
PIRiJC1276.
RefSeqiNP_012706.1. NM_001179781.1.

Genome annotation databases

EnsemblFungiiYKL216W; YKL216W; YKL216W.
GeneIDi853664.
KEGGisce:YKL216W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83295 Genomic DNA. Translation: AAA34566.1.
X59371 Genomic DNA. Translation: CAA42014.1.
AJ585637 Genomic DNA. Translation: CAE52157.1.
AJ585638 Genomic DNA. Translation: CAE52158.1.
AJ585639 Genomic DNA. Translation: CAE52159.1.
AJ585640 Genomic DNA. Translation: CAE52160.1.
AJ585641 Genomic DNA. Translation: CAE52161.1.
AJ585642 Genomic DNA. Translation: CAE52162.1.
AJ585643 Genomic DNA. Translation: CAE52163.1.
AJ585644 Genomic DNA. Translation: CAE52164.1.
AJ585645 Genomic DNA. Translation: CAE52165.1.
AJ585646 Genomic DNA. Translation: CAE52166.1.
AJ585647 Genomic DNA. Translation: CAE52167.1.
AJ585648 Genomic DNA. Translation: CAE52168.1.
AJ585649 Genomic DNA. Translation: CAE52169.1.
AJ585650 Genomic DNA. Translation: CAE52170.1.
AJ585651 Genomic DNA. Translation: CAE52171.1.
X75951 Genomic DNA. Translation: CAA53557.1.
Z28216 Genomic DNA. Translation: CAA82061.1.
BK006944 Genomic DNA. Translation: DAA08953.1.
PIRiJC1276.
RefSeqiNP_012706.1. NM_001179781.1.

3D structure databases

ProteinModelPortaliP28272.
SMRiP28272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33949. 51 interactors.
DIPiDIP-6573N.
IntActiP28272. 2 interactors.
MINTiMINT-709357.

Chemistry databases

BindingDBiP28272.
ChEMBLiCHEMBL5621.

PTM databases

iPTMnetiP28272.

Proteomic databases

MaxQBiP28272.
PRIDEiP28272.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL216W; YKL216W; YKL216W.
GeneIDi853664.
KEGGisce:YKL216W.

Organism-specific databases

EuPathDBiFungiDB:YKL216W.
SGDiS000001699. URA1.

Phylogenomic databases

GeneTreeiENSGT00500000044924.
HOGENOMiHOG000225104.
InParanoidiP28272.
KOiK00226.
OMAiGGISGKC.
OrthoDBiEOG092C37TJ.

Enzyme and pathway databases

UniPathwayiUPA00070.
BioCyciMetaCyc:YKL216W-MONOMER.
YEAST:YKL216W-MONOMER.
ReactomeiR-SCE-500753. Pyrimidine biosynthesis.
SABIO-RKP28272.

Miscellaneous databases

PROiP28272.

Family and domain databases

CDDicd04741. DHOD_1A_like. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00224. DHO_dh_type1. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR033886. DHOD_1A.
IPR005720. Dihydroorotate_DH.
IPR024920. Dihydroorotate_DH_1.
IPR012135. Dihydroorotate_DH_1_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsiTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEiPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYRD_YEAST
AccessioniPrimary (citable) accession number: P28272
Secondary accession number(s): D6VWY7, Q2XN75, Q70DC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 30, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 264000 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: 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.