B4RJT2 · PYRC_NEIG2
- ProteinDihydroorotase
- GenepyrC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids344 (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 | 13 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 15 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 15-17 | substrate | ||||
Sequence: HLR | ||||||
Binding site | 41 | substrate | ||||
Sequence: N | ||||||
Binding site | 98 | Zn2+ 1 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 98 | Zn2+ 2 (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 135 | substrate | ||||
Sequence: H | ||||||
Binding site | 135 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 173 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 218 | substrate | ||||
Sequence: L | ||||||
Active site | 247 | |||||
Sequence: D | ||||||
Binding site | 247 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 251 | substrate | ||||
Sequence: H | ||||||
Binding site | 263 | substrate | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | dihydroorotase activity | |
Molecular Function | zinc ion binding | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | pyrimidine nucleobase 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 > Betaproteobacteria > Neisseriales > Neisseriaceae > Neisseria
Accessions
- Primary accessionB4RJT2
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000100050 | 1-344 | Dihydroorotase | |||
Sequence: MQTLTIIRPDDMHLHLRDGDALKAVAPYTARQMGRAVIMPNLKPPVVSVADALAYKARIMAALPEGSAFEPLMTLYLTDQATPELVREAKAAGIVAFKLYPAGATTNSDSGVTDLFKLIPVLEEMAKQGILFLVHGEVTDPEIDIFDREAAFIGRVMKPVLAQVPNLKVVFEHITTAEAARLVLEAGDNVAASVTPQHLLLNRNDLLVGGVRPHHFCLPVLKRETHRQALVAAVTGEKAHKFFLGTDSAPHAKSAKENACGCAGMFSAMTAIELYAEVFEKAGALDKLEAFASENGARFYGIPENADTITLVKQSQTVPASVPYGDGELVPMRAGGEIGWTVQY | ||||||
Modified residue | 98 | N6-carboxylysine | ||||
Sequence: K |
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length344
- Mass (Da)37,055
- Last updated2008-09-23 v1
- ChecksumDE8AFD2A9D65201B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001050 EMBL· GenBank· DDBJ | ACF29083.1 EMBL· GenBank· DDBJ | Genomic DNA |