A4Z2G7 (PYRD_BRASO) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 49.
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 | Bradyrhizobium sp. (strain ORS278) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 114615 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium![]() |
Protein attributes
| Sequence length | 364 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-Rule MF_00225 |
| Catalytic activity | (S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP-Rule MF_00225 |
| Cofactor | Binds 1 FMN per subunit By similarity. HAMAP-Rule MF_00225 |
| Pathway | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP-Rule MF_00225 |
| Subunit structure | Monomer By similarity. HAMAP-Rule MF_00225 |
| Subcellular location | Cell membrane; Peripheral membrane protein By similarity HAMAP-Rule 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' UMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 'de novo' pyrimidine nucleobase 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 – 364 | 364 | Dihydroorotate dehydrogenase (quinone) HAMAP-Rule MF_00225 | PRO_1000024156 | |||||
Regions | |||||||||
| Nucleotide binding | 61 – 65 | 5 | FMN By similarity | ||||||
| Nucleotide binding | 316 – 317 | 2 | FMN By similarity | ||||||
| Region | 110 – 114 | 5 | Substrate binding By similarity | ||||||
| Region | 243 – 244 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 173 | 1 | Nucleophile By similarity | ||||||
| Binding site | 65 | 1 | Substrate By similarity | ||||||
| Binding site | 85 | 1 | FMN; via amide nitrogen By similarity | ||||||
| Binding site | 139 | 1 | FMN By similarity | ||||||
| Binding site | 170 | 1 | FMN By similarity | ||||||
| Binding site | 170 | 1 | Substrate By similarity | ||||||
| Binding site | 175 | 1 | Substrate By similarity | ||||||
| Binding site | 214 | 1 | FMN By similarity | ||||||
| Binding site | 242 | 1 | FMN; via carbonyl oxygen By similarity | ||||||
| Binding site | 266 | 1 | FMN; via amide nitrogen By similarity | ||||||
| Binding site | 295 | 1 | FMN; via amide nitrogen By similarity | ||||||
Sequences
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References
| [1] | "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia." Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C., Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L., Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z. Sadowsky M.Science 316:1307-1312(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ORS278. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CU234118 Genomic DNA. Translation: CAL80343.1. |
| RefSeq | YP_001208558.1. NC_009445.1. |
3D structure databases | |
| ProteinModelPortal | A4Z2G7. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 114615.BRADO6742. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAL80343; CAL80343; BRADO6742. |
| GeneID | 5119338. |
| KEGG | bra:BRADO6742. |
| PATRIC | 21229335. VBIBraSp122330_6453. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0167. |
| HOGENOM | HOG000225103. |
| KO | K00226. |
| OMA | ALNRMGF. |
| ProtClustDB | PRK05286. |
Enzyme and pathway databases | |
| BioCyc | BSP114615:GJN5-6433-MONOMER. |
| UniPathway | UPA00070; UER00946. |
Family and domain databases | |
| Gene3D | 3.20.20.70. 1 hit. |
| HAMAP | MF_00225. DHO_dh_type2. |
| InterPro | IPR013785. Aldolase_TIM. IPR012135. Dihydroorotate_DH_1_2. IPR005719. Dihydroorotate_DH_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view] |
| 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_BRASO | ||||||||
| Accession | Primary (citable) accession number: A4Z2G7 | ||||||||
| 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 |

Clusters with
