A0A176QBZ2 · A0A176QBZ2_9MICO
- ProteinDihydroorotase
- GenepyrC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids439 (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 | 60 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 62 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 62-64 | substrate | ||||
Sequence: HLR | ||||||
Binding site | 94 | 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 | 235 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 281 | substrate | ||||
Sequence: N | ||||||
Active site | 308 | |||||
Sequence: D | ||||||
Binding site | 308 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 312 | substrate | ||||
Sequence: H | ||||||
Binding site | 326-327 | 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 > Actinomycetota > Actinomycetes > Micrococcales > Intrasporangiaceae > Janibacter
Accessions
- Primary accessionA0A176QBZ2
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 | 52-240 | Dihydroorotase bacterial | ||||
Sequence: VLPGLVDLHTHLREPGREDAETIATGSAAAAVGGFTAILAMANTSPVTDTAEAAERVLDLGRAAGLVDVQPIGAVTKGLDGHELAELGLMHRSRAGVTVFSDDGRCVADARVMRRALEYVRAFDGVVSQHSQDPELAGASACCHEGELSGRLGLPGWPAAAEASIIARDAQLALLTGSRVHVAHVSTAE | ||||||
Domain | 283-423 | Amidohydrolase-related | ||||
Sequence: PLRPDEDVAALREGLADGTIDAVATDHAPHARHDKEHAFVDAAFGMTGLETAFAVVHDVMVRQGSMDLAGLARVMSSAPARIAGLAEHGGELVVGAPAHLALVDPGATVTVDRAATASLSRNTPFHGRTLTGSVVATVLRG |
Sequence similarities
Family and domain databases
Sequence
- Sequence statusComplete
- Length439
- Mass (Da)45,405
- Last updated2016-09-07 v1
- Checksum20B82F117E5BBC1F
Keywords
- Technical term