A0AAD9JF74 · A0AAD9JF74_9ANNE
- ProteinDihydroorotase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2193 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
Catalytic activity
- (S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate + H+
Cofactor
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 219 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 303 | |||||
Sequence: H | ||||||
Active site | 305 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | amino acid binding | |
Molecular Function | aspartate carbamoyltransferase activity | |
Molecular Function | ATP binding | |
Molecular Function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity | |
Molecular Function | dihydroorotase activity | |
Molecular Function | metal ion binding | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | citrulline biosynthetic process | |
Biological Process | glutamine metabolic process | |
Biological Process | UTP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameDihydroorotase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Annelida > Polychaeta > Sedentaria > Canalipalpata > Terebellida > Terebelliformia > Alvinellidae > Paralvinella
Accessions
- Primary accessionA0AAD9JF74
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 486-678 | ATP-grasp | ||||
Sequence: ASKMAEINEPVSPSEAAYNVEQALGAAGRLGYPVMIRAAFALGGLGSGFADTPAQLESLANTAFAHTNQILVDKSLKGWKEVEYEVIRDAYDNCITVCNMENVDPLGIHTGESIVVAPSQTLSNVDYYMLRSTAIKVIRHLGIVGECNIQYALSPQSQQYYIIEVNARLSRSSALASKATGYPLAYISAKLAL | ||||||
Domain | 1020-1206 | ATP-grasp | ||||
Sequence: SRMLDNMGISQPLWRELTDIETAKTFCEEVGFPCLVRPSYVLSGAAMNVAHSRHDLEDYLKQASDVSKEHPVVISKFILEAKEIDVDAVAVEGEVLCMAVCEHVENAGLHSGDATLVTPPQDLNNETLQKIRQICCAISQALEVTGPLNLQLIAKVIECNVRVSRSFPFVSKTLGHDFVAMATQAII | ||||||
Domain | 1271-1428 | MGS-like | ||||
Sequence: FKYPKKNILLSIGSYRQKSELLATVHTLEEMGYNLYASRGTADFYSEHGVKVKEVDWPYEDTGDKSKCNGFHQCTIADYLSENKFDLVINLPMRNSGGRAASSFITQGYKTRRMAVDYSVPLITDVKCTKLLVEAMRRLQQPPKLKTDIDCLTSQRVV | ||||||
Region | 1795-1816 | Disordered | ||||
Sequence: LLSPSHRNSTSSTTKFAMPPSV |
Sequence similarities
In the 2nd section; belongs to the CarB family.
In the 3rd section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.
In the C-terminal section; belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
In the N-terminal section; belongs to the CarA family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,193
- Mass (Da)242,987
- Last updated2024-05-29 v1
- ChecksumEDE6B0F4978EDAD3
Keywords
- Technical term