The domain within your query sequence starts at position 57 and ends at position 156; the E-value for the DHDPS domain shown below is 5.8e-11.



PFAM accession number:PF00701
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 process:metabolic process (GO:0008152)
GO function:lyase activity (GO:0016829)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry DHDPS