A3N0D6 (PYRD_ACTP2) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 40.
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) EC=1.3.5.2 Alternative name(s): DHOdehase Short name=DHOD Short name=DHODase Dihydroorotate oxidase | ||||
| Gene names |
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| Organism | Actinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 416269 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus |
Protein attributes
| Sequence length | 335 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity. HAMAP MF_00225 |
| Catalytic activity | (S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP MF_00225 |
| Cofactor | Binds 1 FMN per subunit By similarity. HAMAP MF_00225 |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP MF_00225 |
| Subunit structure | Monomer By similarity. HAMAP MF_00225 |
| Subcellular location | Cell membrane; Peripheral membrane protein By similarity HAMAP MF_00225. |
| 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 |
| Cellular component | plasma membrane Inferred 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 335 | 335 | Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225 | PRO_1000024146 | |||||
Regions | |||||||||
| Nucleotide binding | 58 – 62 | 5 | FMN By similarity | ||||||
| Nucleotide binding | 314 – 315 | 2 | FMN By similarity | ||||||
| Region | 107 – 111 | 5 | Substrate binding By similarity | ||||||
| Region | 242 – 243 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 171 | 1 | Nucleophile By similarity | ||||||
| Binding site | 62 | 1 | Substrate By similarity | ||||||
| Binding site | 82 | 1 | FMN; via amide nitrogen By similarity | ||||||
| Binding site | 135 | 1 | FMN By similarity | ||||||
| Binding site | 168 | 1 | FMN By similarity | ||||||
| Binding site | 168 | 1 | Substrate By similarity | ||||||
| Binding site | 173 | 1 | Substrate By similarity | ||||||
| Binding site | 213 | 1 | FMN By similarity | ||||||
| Binding site | 241 | 1 | FMN; via carbonyl oxygen By similarity | ||||||
| Binding site | 264 | 1 | FMN; via amide nitrogen By similarity | ||||||
| Binding site | 293 | 1 | FMN; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)." Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E. J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: L20. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000569 Genomic DNA. Translation: ABN73872.1. |
| RefSeq | YP_001053477.1. NC_009053.1. |
3D structure databases | |
| ProteinModelPortal | A3N0D6. |
| SMR | A3N0D6. Positions 2-331. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A3N0D6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4849059. |
| GenomeReviews | Gene locus APL_0774 in contig CP000569_GR. |
| KEGG | apl:APL_0774. |
| PATRIC | 20746424. VBIActPle94089_0809. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0167. |
| HOGENOM | HBG351027. |
| OMA | SYVTVNI. |
| PhylomeDB | A3N0D6. |
| ProtClustDB | PRK05286. |
Enzyme and pathway databases | |
| BioCyc | APLE416269:APL_0774-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00225. DHO_dh_type2. [Tree] |
| 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] |
| PIRSF | PIRSF000164. DHO_oxidase. 1 hit. |
| TIGRFAMs | TIGR01036. PyrD_sub2. 1 hit. |
| PROSITE | PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PYRD_ACTP2 | ||||||||
| Accession | Primary (citable) accession number: A3N0D6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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