O27199 · PYRC_METTH
- ProteinDihydroorotase
- GenepyrC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids431 (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 | 55 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 57 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 57-59 | substrate | ||||
Sequence: HFR | ||||||
Binding site | 89 | substrate | ||||
Sequence: N | ||||||
Binding site | 139 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 139 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 169 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 223 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 290 | |||||
Sequence: D | ||||||
Binding site | 290 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 294 | substrate | ||||
Sequence: H | ||||||
Binding site | 308-309 | substrate | ||||
Sequence: PG |
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
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDihydroorotase
- EC number
- Short namesDHOase
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Methanomada group > Methanobacteria > Methanobacteriales > Methanobacteriaceae > Methanothermobacter
Accessions
- Primary accessionO27199
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000147273 | 1-431 | Dihydroorotase | |||
Sequence: MFDLSLENCRVDRDLTVNIGVDDGKIVQISRGRIDASEKIDLKGYFVLPGLIDAHVHFRDPGLEYKEDFRTGSMAAAHGGFSTVLDMPNTVPPADNAAEFERKIRIGERKSVVDFGLHAGFRSVSDVKGILRFMPASFKVFMDLTGISTVDGLFRELKDLSAPVPVTVHCENRDVVMKSMKELKDRSDPSAYALARPPLAEEVSVAEVLALSIHHEHPVHICHLSTVKALQLVEPFREYVTCEVTPHHLLLDSGAFRRFGTMVKTNPPLRPPESRIYPEFLDRINIIGTDHAPHGIEEKRKGIWDAPPGIPNLEVVLKLLLTLVSKGRMSLSTIRRMLAEEPARIFGLRSKGRIAEGMDADFTVIDLKETGRIRSDEFYSKAHYTPFEGFSYTGGPVMTIVRGRAVMRDGEVLEGNGRYIPAEHDGKHGSA | ||||||
Modified residue | 139 | N6-carboxylysine | ||||
Sequence: K |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length431
- Mass (Da)47,946
- Last updated2003-02-01 v2
- ChecksumFFE05E8B923ADAF9
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1-2 | in Ref. 2; AAA73440 | ||||
Sequence: MF → SL | ||||||
Sequence conflict | 44 | in Ref. 2; AAA73440 | ||||
Sequence: G → A | ||||||
Sequence conflict | 133 | in Ref. 2; AAA73440 | ||||
Sequence: F → N | ||||||
Sequence conflict | 195-201 | in Ref. 2; AAA73440 | ||||
Sequence: ARPPLAE → CKTSPRR | ||||||
Sequence conflict | 242-243 | in Ref. 2; AAA73440 | ||||
Sequence: CE → SQ | ||||||
Sequence conflict | 343 | in Ref. 2; AAA73440 | ||||
Sequence: A → P | ||||||
Sequence conflict | 395-404 | in Ref. 2; AAA73440 | ||||
Sequence: GPVMTIVRGR → ARHDHCQGQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE000666 EMBL· GenBank· DDBJ | AAB85616.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
U09990 EMBL· GenBank· DDBJ | AAA73440.1 EMBL· GenBank· DDBJ | Genomic DNA |