CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.30 | 2-Layer Sandwich | |
3.30.1490 | Dna Ligase; domain 1 | |
3.30.1490.20 | ATP-grasp fold, A domain |
Domain Context
CATH Clusters
Superfamily | ATP-grasp fold, A 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.
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UniProtKB Entries (1)
P0A6F1 |
CARA_ECOLI
Escherichia coli K-12
Carbamoyl-phosphate synthase small chain
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PDB Structure
PDB | 1A9X |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis.
Biochemistry
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