P72170 · PYRC_PSEAE
- ProteinDihydroorotase
- GenepyrC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids348 (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 | 14 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 16 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 16-18 | substrate | ||||
Sequence: HLR | ||||||
Binding site | 42 | substrate | ||||
Sequence: N | ||||||
Binding site | 100 | Zn2+ 1 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 100 | Zn2+ 2 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 137 | substrate | ||||
Sequence: H | ||||||
Binding site | 137 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 175 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 220 | substrate | ||||
Sequence: L | ||||||
Active site | 248 | |||||
Sequence: D | ||||||
Binding site | 248 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 252 | substrate | ||||
Sequence: H | ||||||
Binding site | 264 | substrate | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | dihydroorotase activity | |
Molecular Function | zinc ion binding | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | pyrimidine nucleotide biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDihydroorotase
- EC number
- Short namesDHOase
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionP72170
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000147212 | 1-348 | Dihydroorotase | |||
Sequence: MSDRLTLLRPDDWHIHLRDGAALANTVGDAARTFGRAIVMPNLVPPVRNAAEADAYRQRILAARPAASRFEPLMVLYLTDRTSTEEIRTAKASGFVHAAKLYPAGATTNSDSGVTRIDNIFEALEAMAEVGMPLLVHGEVTRAEVDVFDREKQFIDEHLRRVVERFPTLKVVFEHITTGDAAQFVREAPANVGATITAHHLLYNRNHMLVGGIRPHFYCLPILKRNTHQEALLDAAVSGNPKFFLGTDSAPHARHAKEAACGCAGCYSAYAAIELYAEAFEQRNALDKLEGFASLHGPDFYGLPRNTDRITLVREEWQAPASLPFGDFDVVPLRAGETLRWKLLEAGA | ||||||
Modified residue | 100 | N6-carboxylysine | ||||
Sequence: K |
Proteomic databases
Interaction
Structure
Family & Domains
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length348
- Mass (Da)38,407
- Last updated2000-05-30 v2
- Checksum6E3EF751A5B4DDB8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U73505 EMBL· GenBank· DDBJ | AAC73109.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE004091 EMBL· GenBank· DDBJ | AAG06915.1 EMBL· GenBank· DDBJ | Genomic DNA |