Q74J32 · PYRC_LACJO
- ProteinDihydroorotase
- GenepyrC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids425 (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 | 56 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 58 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 58-60 | substrate | ||||
Sequence: HYR | ||||||
Binding site | 90 | substrate | ||||
Sequence: N | ||||||
Binding site | 148 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 148 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 175 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 228 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 274 | substrate | ||||
Sequence: N | ||||||
Active site | 301 | |||||
Sequence: D | ||||||
Binding site | 301 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 305 | substrate | ||||
Sequence: H | ||||||
Binding site | 319-320 | 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 > Lactobacillales > Lactobacillaceae > Lactobacillus
Accessions
- Primary accessionQ74J32
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000024090 | 1-425 | Dihydroorotase | |||
Sequence: MTTVIKNGTVYQNGHLIKADVLIDGQKIKAIGTDLEGEEIIDASGMIVSPGLVDVHVHYRDPGQTYKEDIKTGSQAAARGGFTTVGAMPNVTPVPNTAELMDKMVRENQKKGLVHILQYGPVTNDETTDIIPDYAALKKAGAFALSNDGHGVQSAQTMYLAMQKAKENNLIIAAHAQDDSLFNKGIVNEGIAAEKLDLPPVTELAETTQIARDLLLAQKTGVHYHICHVSTKTSVELVRLAKARGIKVTCEVAPHHILLTDSDIPEDNAYFKMNPPLRSKEDQVALLVGLLDGTIDLIATDHAPHAKAEKQGGMRGAAFGITGSETAFSTLYTRFVKEEKVFTLEQLLSLLTDKPATVFGIENAGLLAPGENADIAIFDIEHQREIKEDDFKSKGVNTPFTGHKVYGETVMTFVDGKVVYQRGTK |
Structure
Family & Domains
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length425
- Mass (Da)46,053
- Last updated2004-07-05 v1
- Checksum99C2F52414311027
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE017198 EMBL· GenBank· DDBJ | AAS09099.1 EMBL· GenBank· DDBJ | Genomic DNA |