CATH Domain 1vi1A00

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.40	3-Layer(aba) Sandwich
	3.40.718	Isopropylmalate Dehydrogenase
	3.40.718.10	Isopropylmalate Dehydrogenase

Domain Context

CATH Clusters

Superfamily	Isopropylmalate Dehydrogenase
Functional Family

Enzyme Information

2.3.1.274

Phosphate acyltransferase.

based on mapping to UniProt P71018

An acyl-[acyl-carrier protein] + phosphate = an acyl phosphate + an [acyl-carrier protein].

-!- The enzyme, found in bacteria, catalyzes the synthesis of fatty acyl- phosphate from acyl-[acyl carrier protein], a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. -!- While the activity is modestly enhanced by Mg(2+), the enzyme does not require a divalent cation. -!- Formerly EC 2.3.1.n2.

UniProtKB Entries (1)

P71018

PLSX_BACSU

Bacillus subtilis subsp. subtilis str. 168

Phosphate acyltransferase

PDB Structure

PDB	1VI1
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Structural analysis of a set of proteins resulting from a bacterial genomics project Badger, J., Sauder, J.M., Adams, J.M., Antonysamy, S., Bain, K., Bergseid, M.G., Buchanan, S.G., Buchanan, M.D., Batiyenko, Y., Christopher, J.A., Emtage, S., Eroshkina, A., Feil, I., Furlong, E.B., Gajiwala, K.S., Gao, X., He, D., Hendle, J., Huber, A., Hoda, K., Kearins, P., Kissinger, C., Laubert, B., Lewis, H.A., Lin, J., Loomis, K., Lorimer, D., Louie, G., Maletic, M., Marsh, C.D., Miller, I., Molinari, J., Muller-Dieckmann, H.J., Newman, J.M., Noland, B.W., Pagarigan, B., Park, F., Peat, T.S., Post, K.W., Radojicic, S., Ramos, A., Romero, R., Rutter, M.E., Sanderson, W.E., Schwinn, K.D., Tresser, J., Winhoven, J., Wright, T.A., Wu, L., Xu, J., Harris, T.J. Proteins