CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 3 | Alpha Beta | 
|   | 3.20 | Alpha-Beta Barrel | 
|   | 3.20.20 | TIM Barrel | 
|   | 3.20.20.140 | Metal-dependent hydrolases | 
Domain Context
CATH Clusters
| Superfamily | Metal-dependent hydrolases | 
| Functional Family | CAD protein isoform X2 | 
Enzyme Information
| 6.3.5.5 | Carbamoyl-phosphate synthase (glutamine-hydrolyzing). based on mapping to UniProt P27708 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. -!- The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. -!- The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. -!- The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. -!- The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. -!- The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. -!- The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. -!- Cf. EC 6.3.4.16. -!- Formerly EC 2.7.2.9. | 
| 2.1.3.2 | Aspartate carbamoyltransferase. based on mapping to UniProt P27708 Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate. | 
| 3.5.2.3 | Dihydroorotase. based on mapping to UniProt P27708 (S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate. | 
UniProtKB Entries (1)
| P27708 | PYR1_HUMAN Homo sapiens CAD protein | 
PDB Structure
| PDB | 4C6P | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | Structure, Functional Characterization and Evolution of the Dihydroorotase Domain of Human Cad. Structure | 
