CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.50 | Rossmann fold | |
3.40.50.880 | Class I glutamine amidotransferase (GATase) domain |
Domain Context
CATH Clusters
Superfamily | 3.40.50.880 |
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
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PDB Structure
PDB | 5TKV |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Human CTP synthase filament structure reveals the active enzyme conformation.
Nat. Struct. Mol. Biol.
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