Protein Family Models

This family has a TIM barrel structure. [1]. 7853400. The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution. Mirwaldt C, Korndorfer I, Huber R;. J Mol Biol 1995;246:227-239. [1]. 8081752. The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli. Izard T, Lawrence MC, Malby RL, Lilley GG, Colman PM;. Structure 1994;2:361-369. (from Pfam)

Date:

2024-10-16

4-hydroxy-tetrahydrodipicolinate synthase family protein may catalyze a key step in lysine biosynthesis, the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue

Date:

2024-07-16

Members of this family are 4-hydroxy-tetrahydrodipicolinate synthase, previously (incorrectly) called dihydrodipicolinate synthase. It is a homotetrameric enzyme of lysine biosynthesis. E. coli has several paralogs closely related to dihydrodipicoline synthase (DapA), as well as the more distant N-acetylneuraminate lyase. In Pyrococcus horikoshii, the bidirectional best hit with E. coli is to an uncharacterized paralog of DapA, not DapA itself, and it is omitted from the seed. The putative members from the Chlamydias (pathogens with a parasitic metabolism) are easily the most divergent members of the multiple alignment.

Gene:

dapA

Date:

2021-04-27