A0A934TNJ1 · A0A934TNJ1_9BURK
- ProteinDihydroorotase
- GenepyrC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids344 (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 | 14 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 16 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 16-18 | substrate | |||
Binding site | 42 | substrate | |||
Binding site | 99 | Zn2+ 1 (UniProtKB | ChEBI); via carbamate group | |||
Binding site | 99 | Zn2+ 2 (UniProtKB | ChEBI); via carbamate group | |||
Binding site | 136 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 136 | substrate | |||
Binding site | 174 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 219 | substrate | |||
Active site | 247 | ||||
Binding site | 247 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 251 | substrate | |||
Binding site | 263 | substrate | |||
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 | pyrimidine ribonucleotide 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 > Betaproteobacteria > Burkholderiales > Comamonadaceae > Ramlibacter
Accessions
- Primary accessionA0A934TNJ1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 99 | N6-carboxylysine | |||
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 12-310 | Amidohydrolase-related | |||
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length344
- Mass (Da)37,737
- Last updated2023-02-22 v1
- Checksum7ABF19A1C9A3E627
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAEPWM010000001 EMBL· GenBank· DDBJ | MBK6004497.1 EMBL· GenBank· DDBJ | Genomic DNA |