F8IH90 · F8IH90_ALIAT
- ProteinDihydroorotase
- GenepyrC
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids431 (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 | 62 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 64 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 64-66 | substrate | ||||
Sequence: HLR | ||||||
Binding site | 96 | substrate | ||||
Sequence: N | ||||||
Binding site | 154 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 154 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 181 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 233 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 279 | substrate | ||||
Sequence: N | ||||||
Active site | 306 | |||||
Sequence: D | ||||||
Binding site | 306 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 310 | substrate | ||||
Sequence: H | ||||||
Binding site | 324-325 | substrate | ||||
Sequence: FG |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | allantoinase activity | |
Molecular Function | dihydroorotase activity | |
Molecular Function | zinc ion binding | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | purine nucleobase catabolic 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
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Alicyclobacillaceae > Alicyclobacillus
Accessions
- Primary accessionF8IH90
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 54-421 | Amidohydrolase-related | ||||
Sequence: VLPGFVDVHVHLRDPGLTHKETLASGLQAAAAGGFTQVACMPNTKPPIARAEIVEDIIRRGEAIGKAEVHPIACLTLDQEGEALADYEALAEAGAMGFSDDGRGVQDGGLMREALAKLAALGKPAMIHAEDESISRGGALHERAAARLGTTAQPGSAEAAMIARDILLAEETGAHLHVCHVSREASAALVQFGKRRGIRVTAEVTPHHLLLSERDIQSADANWKVNPPLASEEDRRACLVAFADGTLDIIATDHAPHHPDEKAKGMDEAPFGMVGLEMAFALLYTGLVCEGLVPMRRLVEAMSERPCRLFGLEGGQIRPGARADLVLVDLGRRWTIDPSTLYTKGRNTPFAGQSVVGKVIETIRAGRV |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length431
- Mass (Da)46,122
- Last updated2011-09-21 v1
- Checksum9ECF6201CF052152
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP002902 EMBL· GenBank· DDBJ | AEJ43175.1 EMBL· GenBank· DDBJ | Genomic DNA |