A0A5P9QBT1 · A0A5P9QBT1_9MICO
- ProteinDihydroorotate dehydrogenase (quinone)
- GenepyrD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids356 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic activity
- (S)-dihydroorotate + a quinone = a quinol + orotate
Cofactor
Note: Binds 1 FMN per subunit.
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 78 | substrate | ||||
Sequence: K | ||||||
Binding site | 98 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 123-127 | substrate | ||||
Sequence: NRMGF | ||||||
Binding site | 156 | FMN (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 189 | FMN (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 189 | substrate | ||||
Sequence: N | ||||||
Active site | 192 | Nucleophile | ||||
Sequence: S | ||||||
Binding site | 194 | substrate | ||||
Sequence: N | ||||||
Binding site | 235 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 263 | FMN (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 264-265 | substrate | ||||
Sequence: NT | ||||||
Binding site | 278 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 307 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 328-329 | FMN (UniProtKB | ChEBI) | ||||
Sequence: YT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | dihydroorotate dehydrogenase (quinone) activity | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | 'de novo' UMP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydroorotate dehydrogenase (quinone)
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Luteimicrobium
Accessions
- Primary accessionA0A5P9QBT1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 59-347 | Dihydroorotate dehydrogenase catalytic | ||||
Sequence: VQALGRSFPAPLGLAGGFDKDALAVRGLATIGFAFVEIGTVTAHAQPGNEKPRLFRVLDQRAIRNRMGFNNRSAAAAAERLKRLRRTSGGRAVVVGANIGKTKVTPSADAAADYATSAGLLAPHADYLVVNVSSPNTPGLRDLQSVESLRPILVAVREAADTATTGSGGPRVPLLVKIAPDLVDDDVDAVADLVLELGLDGVVAVNTTIAHDLGPGGLSGPPLLPRGLDVVRRLRERLGAGPVIIGVGGITTVDDARAYLEAGADLLQGYTAFIYEGPFWASRINRALT |
Sequence similarities
Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length356
- Mass (Da)37,221
- Last updated2020-04-22 v1
- ChecksumBEC1B3DA9717BA97
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP045529 EMBL· GenBank· DDBJ | QFU98590.1 EMBL· GenBank· DDBJ | Genomic DNA |