A0A2M8WKN3 · A0A2M8WKN3_9RHOB
- ProteinDihydroorotase
- GenepyrC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids350 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic activity
- (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate + H+
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 18 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 20 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 20-22 | substrate | ||||
Sequence: HLR | ||||||
Binding site | 46 | substrate | ||||
Sequence: N | ||||||
Binding site | 104 | Zn2+ 1 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 104 | Zn2+ 2 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 141 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 141 | substrate | ||||
Sequence: H | ||||||
Binding site | 179 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 224 | substrate | ||||
Sequence: L | ||||||
Active site | 252 | |||||
Sequence: D | ||||||
Binding site | 252 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 256 | substrate | ||||
Sequence: H | ||||||
Binding site | 268 | substrate | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | dihydroorotase activity | |
Molecular Function | zinc ion binding | |
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 nameDihydroorotase
- EC number
- Short namesDHOase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Paracoccaceae > Yoonia
Accessions
- Primary accessionA0A2M8WKN3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 104 | N6-carboxylysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-314 | Amidohydrolase-related | ||||
Sequence: DWHLHLRDGEMLKAVLPETTRHFARAIIMPNLVPPVVTAEQAVAYRTRIMAAVPEGARFTPLMTLYLTEATDPEDVRAAHADAIATAVKLYPAGATTNSASGVRDFEKVRPVLEVMAEIGMPLCVHGEVTDSQIDIFDREAVFIEKVLKPLRKKVPDLKIVMEHVTTQNAVDYVRDSHKNMAATITTHHLIINRNHILAGGIKPHFYCLPVAKREAHRVALVQAAVSGDKRFFLGTDSAPHTDPLKLQACGCAGIFTAPNTMSCLAEVFDAAGRITKLEDFTSLNGPRFYGLPPNEETI |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length350
- Mass (Da)38,610
- Last updated2018-04-25 v1
- ChecksumD623BF87FD6D5856