Reviewed,
UniProtKB/Swiss-Prot Q39GX5 (PYRD_BURS3)
Last modified
November 25, 2008.
Version 31.
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 EC=1.3.3.1 Alternative name(s): Dihydroorotate oxidase DHOdehase Short name=DHODase Short name=DHOD | ||||
| Gene names |
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| Organism | Burkholderia sp. (strain 383) (Burkholderia cepacia (strain ATCC 17760 / NCIB 9086 / R18194)) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 269483 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex |
Protein attributes
| Sequence length | 345 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | (S)-dihydroorotate + O(2) = orotate + H(2)O(2). |
| Cofactor | Binds 1 FMN per subunit By similarity. |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cell membrane; Peripheral membrane proteinBy similarity. |
| Sequence similarities | Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily. |
Ontologies
Keywords | |
|---|---|
| Biological process | Pyrimidine biosynthesis |
| Cellular component | Cell membrane Membrane |
| 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 oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | plasma membrane Inferred from electronic annotation. Source: HAMAP |
| Molecular function | dihydroorotate oxidase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Complete sequence of chromosome 1 of Burkholderia sp. 383." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P. Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000151 Genomic DNA. Translation: ABB08291.1. Different initiation. | |
| RefSeq | YP_368935.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3749902. |
| GenomeReviews | Gene locus Bcep18194_A4696 in contig CP000151_GR. |
| KEGG | bur:Bcep18194_A4696. |
| NMPDR | fig|269483.3.peg.6238. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q39GX5. |
Enzyme and pathway databases | |
| BioCyc | BSP36773:BCEP18194_A4696-MON. |
Family and domain databases | |
| HAMAP | MF_00225. [Tree] |
| InterPro | IPR013785. Aldolase_TIM. IPR012135. DHO_DHase_1_2. IPR005719. DHO_DHase_2. IPR001295. Dihydroorotate_DHase_core. [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 | TIGR01036. pyrD_sub2. 1 hit. |
| PROSITE | PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYRD_BURS3 | ||||||||
| Accession | Primary (citable) accession number: Q39GX5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


