Dihydrodipicolinate synthetase family
SMART accession number:SM01130
Description: This family has a TIM barrel structure. This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds.
Interpro abstract (IPR002220):

Dihydrodipicolinate synthase (EC (DHDPS, DapA) catalyses, in higher plants, some fungi and bacteria (gene dapA), the first reaction specific to the biosynthesis of lysine and of diaminopimelate [ (PUBMED:22949190) ]. DHDPS is responsible for the condensation of aspartate semialdehyde and pyruvate by a ping-pong mechanism in which pyruvate first binds to the enzyme by forming a Schiff-base with a lysine residue [ (PUBMED:1463470) (PUBMED:20025926) ].

Other proteins are structurally related to DHDPS and probably also act via a similar catalytic mechanism [ (PUBMED:9047371) ]:

  • Escherichia coli N-acetylneuraminate lyase (EC (gene nanA), which catalyses the condensation of N-acetyl-D-mannosamine and pyruvate to form N-acetylneuraminate.
  • Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase.
  • D-4-deoxy-5-oxoglucarate dehydratase.
  • Rhizobium meliloti protein mosA [ (PUBMED:8349559) ], which is involved in the biosynthesis of the rhizopine 3-o-methyl-scyllo-inosamine.
  • Thermoproteus tenax 2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase (KdgA) [ (PUBMED:18186475) ].
GO function:lyase activity (GO:0016829)
Family alignment:
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There are 57397 DHDPS domains in 57392 proteins in SMART's nrdb database.

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