A0A0N8GHG0 · A0A0N8GHG0_9BACI
- ProteinDihydroorotase
- GenepyrC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids428 (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 | 59 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 61 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 61-63 | substrate | ||||
Sequence: HLR | ||||||
Binding site | 93 | substrate | ||||
Sequence: N | ||||||
Binding site | 151 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 151 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 178 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 231 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 277 | substrate | ||||
Sequence: N | ||||||
Active site | 304 | |||||
Sequence: D | ||||||
Binding site | 304 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 308 | substrate | ||||
Sequence: H | ||||||
Binding site | 322-323 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Rossellomorea
Accessions
- Primary accessionA0A0N8GHG0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 50-420 | Amidohydrolase-related | ||||
Sequence: VISPGFVDLHVHLREPGGEYKETIETGTKSAAKGGFTTIAAMPNTRPVPDSVENLQSLNQKISDTAGVRVLPYAAITERQIGNKLNDLPSLKENGAFAFTDDGVGVQSADMMYQAMKMAAGINASIVAHCEENTLIYGGAVHDGTFSKEHNLPGIPSICEAVHISRDVLLAEAAGVHYHVCHISTKESVRVVRDAKKAGINVTAEVTPHHLLLSEDDIPGLDPNFKMNPPLRSKEDRQALIEGLLDGTIDFIATDHAPHTEAEKSEGMQLAPFGIVGLETAFPLLYTNFVEKGIFTLKQLIDWMTIKPSSAFNLPFGLLEVGGEADFTLIDLQEQKEIDPAGFVSKGKNTPFKGWECKGWPKATFYQGSLV |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length428
- Mass (Da)46,727
- Last updated2016-01-20 v1
- ChecksumB90957307C53242B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
LIXZ01000001 EMBL· GenBank· DDBJ | KPL61194.1 EMBL· GenBank· DDBJ | Genomic DNA |