CATH Classification

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
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