CATH Domain 1vi2B01

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.40	3-Layer(aba) Sandwich
	3.40.50	Rossmann fold
	3.40.50.10860	Leucine Dehydrogenase, chain A, domain 1

Domain Context

CATH Clusters

Superfamily	Leucine Dehydrogenase, chain A, domain 1
Functional Family	Quinate/shikimate dehydrogenase

Enzyme Information

1.1.1.282

Quinate/shikimate dehydrogenase.

based on mapping to UniProt P0A6D5

(1) L-quinate + NAD(P)(+) = 3-dehydroquinate + NAD(P)H. (2) Shikimate + NAD(P)(+) = 3-dehydroshikimate + NAD(P)H.

-!- The enzyme is found in bacteria (mostly, but not exclusively, Gram- positive bacteria), fungi, and plants. -!- It participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. -!- While the enzyme can act on both quinate and shikimate, activity is higher with the former.

UniProtKB Entries (1)

P0A6D5

YDIB_ECOLI

Escherichia coli K-12

Quinate/shikimate dehydrogenase

PDB Structure

PDB	1VI2
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