CATH Classification

Domain Context

CATH Clusters

Superfamily Ribonuclease E inhibitor RraA/RraA-like
Functional Family

Enzyme Information
Oxaloacetate decarboxylase.
based on mapping to UniProt Q9KPK1
Oxaloacetate = pyruvate + CO(2).
-!- The enzymes from the fish Gadus morhua (Atlantic cod) and the bacterium Micrococcus luteus prefer Mn(2+), while those from the bacteria Pseudomonas putida and Pseudomonas aeruginosa prefer Mg(2+). -!- Unlike EC, there is no evidence of the enzyme's involvement in Na(+) transport. -!- Formerly EC
4-hydroxy-4-methyl-2-oxoglutarate aldolase.
based on mapping to UniProt Q9KPK1
(1) 4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate. (2) 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate.
-!- This enzyme participates in the degradation of protocatechuate (via the meta-cleavage pathway), phthalate, syringate and gallate. -!- The enzyme from Pseudomonas ochraceae can also cleave 4-hydroxy-2- oxoglutarate to glyoxylate and pyruvate, and also catalyzes the reaction of EC

UniProtKB Entries (1)

Vibrio cholerae O1 biovar El Tor str. N16961
Putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase

PDB Structure

External Links
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.