Reviewed,
UniProtKB/Swiss-Prot Q7Z892 (PYRD1_SACKL)
Last modified
September 1, 2009.
Version 43.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 |
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| Organism | Saccharomyces kluyveri (Yeast) (Saccharomyces silvestris) | ||
| Taxonomic identifier | 4934 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Lachancea |
Protein attributes
| Sequence length | 314 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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 | |
| 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 process | Pyrimidine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | FMN Flavoprotein |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | 'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro UMP biosynthetic processInferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | dihydroorotate oxidase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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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 | |
| SMR | Q7Z892. Positions 5-314. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.3.3.1. 274780. |
Family and domain databases | |
| InterPro | IPR013785. Aldolase_TIM. IPR012135. Dihydroorotate_DH_1_2. IPR005720. Dihydroorotate_DH_1_core. IPR001295. Dihydroorotate_DH_CS. [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 | PYRD1_SACKL | ||||||||
| Accession | Primary (citable) accession number: Q7Z892 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


