Q6CTX8 (PYRD2_KLULA) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 66.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Dihydroorotate dehydrogenase (quinone), mitochondrial Short name=DHOD Short name=DHODase Short name=DHOdehase EC=1.3.5.2 Alternative name(s): Dihydroorotate oxidase | ||||
| Gene names |
| ||||
| Organism | Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome] | ||||
| Taxonomic identifier | 284590 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces |
Protein attributes
| Sequence length | 445 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity. |
| Catalytic activity | (S)-dihydroorotate + a quinone = orotate + a quinol. |
| Cofactor | Binds 1 FMN per subunit By similarity. |
| Pathway | |
| Subcellular location | Mitochondrion inner membrane By similarity; Single-pass membrane protein Potential. |
| Miscellaneous | K.lactis has two isoforms of DHODase, a cytoplasmic isoform and a mitochondrial isoform. |
| Sequence similarities | Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis |
| Cellular component | Membrane Mitochondrion Mitochondrion inner membrane |
| Domain | Transit peptide Transmembrane Transmembrane helix |
| Ligand | FMN Flavoprotein |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| 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 |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | dihydroorotate oxidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 16 | 16 | Mitochondrion Potential | ||||||
| Chain | 17 – 445 | 429 | Dihydroorotate dehydrogenase (quinone), mitochondrial | PRO_0000029893 | |||||
Regions | |||||||||
| Transmembrane | 39 – 56 | 18 | Helical; Potential | ||||||
| Nucleotide binding | 124 – 128 | 5 | FMN By similarity | ||||||
| Nucleotide binding | 407 – 408 | 2 | FMN By similarity | ||||||
| Region | 173 – 177 | 5 | Substrate binding By similarity | ||||||
| Region | 251 – 256 | 6 | Substrate binding By similarity | ||||||
| Region | 331 – 332 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 254 | 1 | Nucleophile By similarity | ||||||
| Binding site | 128 | 1 | Substrate By similarity | ||||||
| Binding site | 148 | 1 | FMN By similarity | ||||||
| Binding site | 221 | 1 | FMN By similarity | ||||||
| Binding site | 251 | 1 | FMN By similarity | ||||||
| Binding site | 302 | 1 | FMN By similarity | ||||||
| Binding site | 330 | 1 | FMN; via carbonyl oxygen By similarity | ||||||
| Binding site | 356 | 1 | FMN; via amide nitrogen By similarity | ||||||
| Binding site | 386 | 1 | FMN; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. Souciet J.-L.Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR382123 Genomic DNA. Translation: CAH01462.1. |
| RefSeq | XP_452611.1. XM_452611.1. |
3D structure databases | |
| ProteinModelPortal | Q6CTX8. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q6CTX8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2891871. |
| GenomeReviews | Gene locus KLLA0C09240g in contig CR382123_GR. |
| KEGG | kla:KLLA0C09240g. |
Phylogenomic databases | |
| eggNOG | fuNOG05791. |
| HOGENOM | HBG351027. |
| OMA | AALNRMG. |
| OrthoDB | EOG4NS6M1. |
Family and domain databases | |
| InterPro | IPR013785. Aldolase_TIM. IPR012135. Dihydroorotate_DH_1_2. IPR005719. Dihydroorotate_DH_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. |
| KO | K00226. |
| Pfam | PF01180. DHO_dh. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01036. PyrD_sub2. 1 hit. |
| PROSITE | PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYRD2_KLULA | ||||||||
| Accession | Primary (citable) accession number: Q6CTX8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with