AT2G19940.1 :

DomainDescriptionEvalueBitsGAStartEnd
DapB_NDihydrodipicolinate reductase, N-terminus1.1E-051420.804785
Semialdhyde_dhSemialdehyde dehydrogenase, NAD binding domain8.5E-3410521.4048185
Sacchrp_dh_NADPSaccharopine dehydrogenase NADP binding domain3.4E-061625.104990
DXP_reductoisom1-deoxy-D-xylulose 5-phosphate reductoisomerase0.000251121.7049108
NAD_binding_10NAD(P)H-binding 1.4E-072027.2053131
DXP_reductoisom1-deoxy-D-xylulose 5-phosphate reductoisomerase0.14221.70125179
Semialdhyde_dhCSemialdehyde dehydrogenase, dimerisation domain1.6E-226920.90202360

 389

DapB_N
Semialdhyde_dh
Sacchrp_dh_NADP
DXP_reductoisom
NAD_binding_10
DXP_reductoisom
Semialdhyde_dhC


References:

Semialdhyde_dhC
10369777 Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. J Mol Biol 1999;289:991-1002.

Semialdhyde_dh
10369777 Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. J Mol Biol 1999;289:991-1002.

DapB_N
8873595 Interaction of pyridine nucleotide substrates with Escherichia coli dihydrodipicolinate reductase: thermodynamic and structural analysis of binary complexes. Biochemistry 1996;35:13294-13302.
9398235 Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate. Biochemistry 1997;36:15081-15088.
7893645 Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase. Biochemistry 1995;34:3502-3512.

DXP_reductoisom
9707569 A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis. Proc Natl Acad Sci U S A 1998;95:9879-9884.

Sacchrp_dh_NADP

NAD_binding_10