B2AH54 · PYRC_CUPTR
- ProteinDihydroorotase
- GenepyrC
- StatusUniProtKB reviewed (Swiss-Prot)
- 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 = H+ + N-carbamoyl-L-aspartate
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) | ||||
Sequence: H | ||||||
Binding site | 16 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 16-18 | substrate | ||||
Sequence: HLR | ||||||
Binding site | 42 | substrate | ||||
Sequence: N | ||||||
Binding site | 100 | Zn2+ 1 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 100 | Zn2+ 2 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 137 | substrate | ||||
Sequence: H | ||||||
Binding site | 137 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 175 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 220 | substrate | ||||
Sequence: L | ||||||
Active site | 248 | |||||
Sequence: D | ||||||
Binding site | 248 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 252 | substrate | ||||
Sequence: H | ||||||
Binding site | 264 | 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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDihydroorotase
- EC number
- Short namesDHOase
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Cupriavidus
Accessions
- Primary accessionB2AH54
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000100039 | 1-344 | Dihydroorotase | |||
Sequence: MTQKLTITRPDDWHLHLRDGAALAAVLPDTARQFARAIVMPNLKPPVTTVAQAQAYRARILAALPAGMQFEPLMTLYLTDNTGPEEIAAARASGFVHGVKLYPAGATTNSDAGVTDIRRCYPALEAMQRAGLPLLVHGEVTDPAIDIFDREAVFIERVMTPLRRDMPELKVVFEHITTKDAAQYVRDASGPVGATITAHHLLYNRNAIFTGGIRPHYYCLPVLKRETHREALVAAATSGSERFFLGTDSAPHARGLKEHACGCAGCYTALHAMELYAEAFDAAGALDKLEAFASFNGPAFYGLPRNTGTLTLEREDWELPAELPYGDTTLVPLRGGETLRWKAR | ||||||
Modified residue | 100 | N6-carboxylysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Sequence
- Sequence statusComplete
- Length344
- Mass (Da)37,579
- Last updated2008-05-20 v1
- Checksum44B55466A1D3DDD8
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU633749 EMBL· GenBank· DDBJ | CAP63103.1 EMBL· GenBank· DDBJ | Genomic DNA |