A0A0D5NDX9 · A0A0D5NDX9_9BACL
- ProteinDihydroorotate dehydrogenase (quinone)
- GenepyrD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids365 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the conversion of dihydroorotate to orotate with NAD+ as electron acceptor.
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
Catalytic activity
- (S)-dihydroorotate + NAD+ = H+ + NADH + orotate
Cofactor
Note: Binds 1 FMN per subunit.
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD+ route): step 1/1.
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 | 69-73 | FMN (UniProtKB | ChEBI) | ||||
Sequence: AGLDK | ||||||
Binding site | 73 | substrate | ||||
Sequence: K | ||||||
Binding site | 93 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 118-122 | substrate | ||||
Sequence: NRMGF | ||||||
Binding site | 147 | FMN (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 180 | FMN (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 180 | substrate | ||||
Sequence: N | ||||||
Active site | 183 | Nucleophile | ||||
Sequence: S | ||||||
Binding site | 185 | substrate | ||||
Sequence: N | ||||||
Binding site | 226 | FMN (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 254 | FMN (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 255-256 | substrate | ||||
Sequence: NT | ||||||
Binding site | 276 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 305 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 326-327 | FMN (UniProtKB | ChEBI) | ||||
Sequence: YT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | dihydroorotate dehydrogenase (NAD+) activity | |
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 > Bacillota > Bacilli > Bacillales > Paenibacillaceae > Paenibacillus
Accessions
- Primary accessionA0A0D5NDX9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Interaction
Subunit
Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
Monomer.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 52-348 | Dihydroorotate dehydrogenase catalytic | ||||
Sequence: LAVNLFGLQFSHPVGLAAGLDKNAKVGDIFRNIGFSFAEMGTVTPKAQAGNELPRLFRLPPDEALINRMGFNNDGADAMAQRLSAGRKRSIPIAVNIGKNKTTPNEEAHLDYRKCLEKLYPFGDFFVVNISSPNTPDLRALQHGGELRTLLSEVLEEMGIQAARSGSKRKPVLVKIAPDMTDEQLELTIDTIAASGVDGLIATNTTLSRDGLTHRNAGETGGLSGKPLKARSTEIVAAVYKQTGGKLPIIGSGGIFNADDAYDKIRAGASMVEIYTALIYRGPEVLKELTSGLRERL |
Sequence similarities
Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length365
- Mass (Da)39,368
- Last updated2015-05-27 v1
- ChecksumEE79A50F1C98A8C0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP011058 EMBL· GenBank· DDBJ | AJY73360.1 EMBL· GenBank· DDBJ | Genomic DNA |