CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.300 | P-loop containing nucleotide triphosphate hydrolases |
Domain Context
CATH Clusters
| Superfamily | P-loop containing nucleotide triphosphate hydrolases |
| Functional Family | CTP synthase |
Enzyme Information
| 6.3.4.2 |
CTP synthase (glutamine hydrolyzing).
based on mapping to UniProt P0A7E5
ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate.
-!- The enzyme contains three functionally distinct sites: an allosteric GTP-binding site, a glutaminase site where glutamine hydrolysis occurs (cf. EC 3.5.1.2), and the active site where CTP synthesis takes place. -!- The reaction proceeds via phosphorylation of UTP by ATP to give an activated intermediate 4-phosphoryl UTP and ADP. -!- Ammonia then reacts with this intermediate generating CTP and a phosphate. -!- The enzyme can also use ammonia from the surrounding solution.
|
UniProtKB Entries (1)
| P0A7E5 |
PYRG_ECOLI
Escherichia coli K-12
CTP synthase
|
PDB Structure
| PDB | 1S1M |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal Structure of Escherichia coli Cytidine Triphosphate Synthetase, a Nucleotide-Regulated Glutamine Amidotransferase/ATP-Dependent Amidoligase Fusion Protein and Homologue of Anticancer and Antiparasitic Drug Targets
Biochemistry
|