CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.470 | D-amino Acid Aminotransferase; Chain A, domain 1 |
|
3.30.470.20 | ATP-grasp fold, B domain |
Domain Context
CATH Clusters
| Superfamily | ATP-grasp fold, B domain |
| Functional Family |
Enzyme Information
| 6.3.5.5 |
Carbamoyl-phosphate synthase (glutamine-hydrolyzing).
based on mapping to UniProt P00968
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.
|
UniProtKB Entries (1)
| P00968 |
CARB_ECOLI
Escherichia coli K-12
Carbamoyl-phosphate synthase large chain
|
PDB Structure
| PDB | 1KEE |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin.
J.Biol.Chem.
|