AT5G09660.1 :

DomainDescriptionEvalueBitsGAStartEnd
Ldh_1_Nlactate/malate dehydrogenase, NAD binding domain016020.4044186
Semialdhyde_dhSemialdehyde dehydrogenase, NAD binding domain7.5E-061521.404485
3Beta_HSD3-beta hydroxysteroid dehydrogenase/isomerase family6.3E-082020.0047158
Ldh_1_Clactate/malate dehydrogenase, alpha/beta C-terminal domain017022.60188352
Semialdhyde_dhSemialdehyde dehydrogenase, NAD binding domain0.63-121.40212234

 354

Ldh_1_N
Semialdhyde_dh
3Beta_HSD
Ldh_1_C
Semialdhyde_dh


References:

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.

Ldh_1_N
10075524 Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD. J Mol Biol 1999;285:703-712.
12029364 Molecular evolution within the L-malate and L-lactate dehydrogenase super-family. J Mol Evol 2002;54:825-840.

3Beta_HSD
1562516 Structure and tissue-specific expression of 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase genes in human and rat classical and peripheral steroidogenic tissues. J Steroid Biochem Mol Biol 1992;41:421-435.

Ldh_1_C
10075524 Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD. J Mol Biol 1999;285:703-712.