CATH Classification

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 5TKV
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Human CTP synthase filament structure reveals the active enzyme conformation.
Lynch, E.M., Hicks, D.R., Shepherd, M., Endrizzi, J.A., Maker, A., Hansen, J.M., Barry, R.M., Gitai, Z., Baldwin, E.P., Kollman, J.M.
Nat. Struct. Mol. Biol.
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