CATH Domain 2vktA00

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 Q9NRF8

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)

Q9NRF8

PYRG2_HUMAN

Homo sapiens

CTP synthase 2

PDB Structure

PDB	2VKT
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Human Ctp Synthetase 2 - Glutaminase Domain Welin, M., Tresaugues, L., Arrowsmith, C.H., Berglund, H., Busam, R.D., Collins, R., Dahlgren, L.G., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Herman, M.D., Johansson, I., Kallas, A., Karlberg, T., Kotenyova, T., Lehtio, L., Moche, M., Nilsson, M.E., Nyman, T., Persson, C., Sagemark, J., Svensson, L., Thorsell, A.G., Van Den Berg, S., Weigelt, J., Nordlund, P. To be Published