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Reviewed, UniProtKB/Swiss-Prot Q7Z892 (PYRD1_SACKL)

Last modified September 1, 2009. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces kluyveri (Yeast) (Saccharomyces silvestris)
Taxonomic identifier4934 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeLachancea

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + O2 = orotate + H2O2.

Cofactor

Binds 1 FMN per subunit By similarity.

Enzyme regulation

The activity is independent of the presence of oxygen.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (O2 route): step 1/1.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

S.kluyveri has two isoforms of DHODase, a cytoplasmic isoform and a mitochondrial isoform.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
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 componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Dihydroorotate dehydrogenase
PRO_0000148503

Sites

Active site1331Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7Z892-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: C7501535D7800D84

FASTA31434,855
        10         20         30         40         50         60 
MSASLAINFL NHTYENPFMN ASGVHCMSTK ELDELKDSRA GAFITKSSTT SKREGNPEPR 

        70         80         90        100        110        120 
YFSVPLGSIN SMGLPNEGFD YYLKYALEYQ KNGSTSTPLF FSVAGMSVEE NLKMLQKIQD 

       130        140        150        160        170        180 
SDFNGITELN LSCPNVPGKP QVAYDFELTK EILTKVFEFF KKPLGVKLPP YFDFAHFDIM 

       190        200        210        220        230        240 
AGILNQLPLS YVNCINSIGN GLYINVETES VVVKPKNGFG GIGGEYVKPT ALANVRAFYT 

       250        260        270        280        290        300 
RLNPTIKIIG TGGIKTGQDA FEHLLCGATM LQVGTELYKE GVSIFDRLER ELKELMDKKG 

       310 
YTSIEQFRGK LNSL 

« Hide

References

[1]"Contribution of horizontal gene transfer to the evolution of Saccharomyces cerevisiae."
Hall C.R., Brachat S., Dietrich F.S.
Eukaryot. Cell 4:1102-1115(2005) [PubMed: 15947202] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 58438 / CBS 3082 / IFO 1685 / JCM 7257 / NRRL Y-12651.
[2]"Horizontal gene transfer promoted evolution of the ability to propagate under anaerobic conditions in yeasts."
Gojkovic Z., Knecht W., Zameitat E., Warneboldt J., Coutelis J.-B., Pynyaha Y., Neuveglise C., Moeller K., Loeffler M., Piskur J.
Mol. Genet. Genomics 271:387-393(2004) [PubMed: 15014982] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.

Cross-references

Sequence databases

AY323902 Genomic DNA. Translation: AAQ01779.1.
AF452109 Genomic DNA. Translation: AAQ04683.1.

3D structure databases

SMRQ7Z892. Positions 5-314.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.3.3.1. 274780.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005720. Dihydroorotate_DH_1_core.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD1_SACKL
AccessionPrimary (citable) accession number: Q7Z892
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: October 1, 2003
Last modified: September 1, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents