A0AAD8FNK4 · A0AAD8FNK4_BIOPF
- ProteinCAD protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids2244 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
Catalytic activity
- (S)-dihydroorotate + H2O = H+ + N-carbamoyl-L-aspartate
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 | 258 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 342 | |||||
Sequence: H | ||||||
Active site | 344 | |||||
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
- Submitted names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Mollusca > Gastropoda > Heterobranchia > Euthyneura > Panpulmonata > Hygrophila > Lymnaeoidea > Planorbidae > Biomphalaria
Accessions
- Primary accessionA0AAD8FNK4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 520-716 | ATP-grasp | ||||
Sequence: RKIFADKMLEINEFVAPSEAAHSVEQAVQAAERLGYPVLIRAAYALGGLGSGFANSKEELLVLVTAAFAHTTQVLVDKSLQGWKEVEYEVVRDAYDNCITVCNMENVDPLGIHTGESIVVAPSQTLTDAEYNMLRTTAIKVIRHLGIVGECNIQYALNPLSQQYYIIEVNARLSRSSALASKATGYPLAYVAAKLAL | ||||||
Domain | 1060-1251 | ATP-grasp | ||||
Sequence: SRMLDNLNINQPLWKELSTFEAAVAFCDEVGYPCLIRPSYVLSGAAMNVAMNKHDLETFLTQAVAVSKDHPVVISKFIQEAKEIDVDAVASDGEVICIAVSEHVENAGVHSGDATLVTPPQDINSETLAKIKGICCAIGRALEVTGPFNIQLIAKDNHLKVIECNVRVSRSFPFVSKALNYDFIATATHIIM | ||||||
Domain | 1316-1473 | MGS-like | ||||
Sequence: FQIPKKNILISIGSYKHKTELIPTMRTLEKLGYQLFASMGTADFYNEHGFNVRSVDWPYEDTGEDSCKNGEQRTIADYLSEHMFDLVINLPLRNSGSYRASSFITQGYKTRRMAVDYSVPLITDVKCTKLFVEALHQLNAQEPVMKTNIDCLTSQKII | ||||||
Compositional bias | 1838-1857 | Polar residues | ||||
Sequence: LSVQIPGNLPASQGTSEPPS | ||||||
Region | 1838-1888 | Disordered | ||||
Sequence: LSVQIPGNLPASQGTSEPPSPRKNHHQEKSHAPRTPKLSENSPFVFESPEH | ||||||
Compositional bias | 1858-1872 | Basic and acidic residues | ||||
Sequence: PRKNHHQEKSHAPRT |
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 statusFragment
- Length2,244
- Mass (Da)249,075
- Last updated2024-05-29 v1
- Checksum08B41F279F7AD728
Features
Showing features for compositional bias, non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1838-1857 | Polar residues | ||||
Sequence: LSVQIPGNLPASQGTSEPPS | ||||||
Compositional bias | 1858-1872 | Basic and acidic residues | ||||
Sequence: PRKNHHQEKSHAPRT | ||||||
Non-terminal residue | 2244 | |||||
Sequence: L |
Keywords
- Technical term