A5I6W9 · A5I6W9_CLOBH
- ProteinDihydroorotase
- GenepyrC
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids396 (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 | 58 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 60 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 60-62 | substrate | ||||
Sequence: HFR | ||||||
Binding site | 92 | substrate | ||||
Sequence: N | ||||||
Binding site | 149 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 149 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 176 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 213 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 253 | substrate | ||||
Sequence: N | ||||||
Active site | 280 | |||||
Sequence: D | ||||||
Binding site | 280 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 284 | substrate | ||||
Sequence: H | ||||||
Binding site | 294-295 | substrate | ||||
Sequence: PG |
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 > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionA5I6W9
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 49-391 | Amidohydrolase-related | ||||
Sequence: TLLPSFIDMHAHFRDPGFTYKEDILTGSRAAVKGGYTMVNLMANTKPICSSNKEVEYVLEKGKEIGLVDIHQCMSITKDFSGDDISHLDSIDKKVKIISEDGKDVMNTRVLIEAMFKAKEKDLIVMCHSEEHDVTNLDTRLSENLMTWRNIALSEFTDCKVHIAHVSTKESMEYIKNAKKKGLKVTCEVAPHHIALTNKIFYRVNPPLREEEDIKVLIEAIKEDLVDCIGTDHAPHSKEDKLKGSPGISGIETSFSTCYTKLVHNNHISLSKLSKIMSKNPADILGVNNGEIKIGREADLVLVDTKEEYKVKSEEFHSKGKNTPMDGMYLKGRIKVTFKAGCI |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length396
- Mass (Da)44,626
- Last updated2007-06-26 v1
- ChecksumBB5E0FD209158EE4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AM412317 EMBL· GenBank· DDBJ | CAL84801.1 EMBL· GenBank· DDBJ | Genomic DNA |