Active Site

Schiff base-forming aldolase, active site (IPR020625)

Short name: Schiff_base-form_aldolases_AS


This entry represents an active site found in members of a structural superfamily of Schiff base-forming aldolases that catalyse reactions in different biological pathways. This superfamily includes members such as dihydrodipicolinate synthase (DHDPS), N-acetylneuraminate lyase (NAL) and 2-keto-3-deoxygluconate aldolase (KDG aldolase) [PMID: 24677246]. One of the Escherichia coli proteins containing this site, dapA (P0A6L2), was first identified as dihydrodipicolinate synthase (DHDPS) [PMID: 1463470]. Later, it has been identified as 4-hydroxy-tetrahydrodipicolinate synthases (EC: [PMID: 20503968].

Among the putative DHDPS genes annotated in the A. tumefaciens genome, dapA7 gene product has been shown to possess DHDPS enzyme activity and is allosterically inhibited by lysine [PMID: 24677246].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016829 lyase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns