A0A484CAP7 · A0A484CAP7_PERFV
- ProteinUncharacterized protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids2235 (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 | 255 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 339 | |||||
Sequence: H | ||||||
Active site | 341 | |||||
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 | 'de novo' UMP biosynthetic process | |
Biological Process | citrulline biosynthetic process | |
Biological Process | glutamine metabolic process | |
Biological Process | UTP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Perciformes > Percoidei > Percidae > Percinae > Perca
Accessions
- Primary accessionA0A484CAP7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 521-713 | ATP-grasp | ||||
Sequence: VEKMEEINEHVAPSEAALSVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNREELTSLVTSAFAHTSQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGESIVVAPSQTLNDHEYNMLRNTAIKVIRHLGIVGECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLGL | ||||||
Domain | 1057-1248 | ATP-grasp | ||||
Sequence: SRMLDTIGISQPQWKELSDTESAWKFCETVGYPCLVRPSYVLSGAAMNVAYSDSDLEKYLTNAVAVSKEHPVVISKFIQEAKEIDVDAVACDGVVMAIAVSEHVENAGVHSGDATLVTPPQDINQKTMERIKIIVHAIGLELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATQAIV | ||||||
Domain | 1313-1469 | MGS-like | ||||
Sequence: FKIPKKNILLSIGSYKNKSELLPTVQALESMGYDLYASLGTADFYTEHGVKVKAVDWPFEEEDSDCPTKEKQRSIMDYLEENHFDLVINLSMRNSGGRRLSSFVTKGYRTRRMAIDYSVPLIIDIKCTKLFVQALHQIGRTPPVKTHIDCMTSQTLV | ||||||
Region | 1818-1885 | Disordered | ||||
Sequence: TWPTASIHPPEPVKESPRTPEHPRPTPPREGPVRTRAPSPRRLTSESRYLLPPRTHRSSDPGLTPEMV | ||||||
Compositional bias | 1831-1846 | Basic and acidic residues | ||||
Sequence: KESPRTPEHPRPTPPR |
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
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,235
- Mass (Da)247,619
- Last updated2019-06-05 v1
- Checksum9DFEDC4BD91FCB04
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1831-1846 | Basic and acidic residues | ||||
Sequence: KESPRTPEHPRPTPPR |
Keywords
- Technical term