AT1G17745.1 :

DomainDescriptionEvalueBitsGAStartEnd
2-Hacid_dhD-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain012724.6085394
NAD_binding_2NAD binding domain of 6-phosphogluconate dehydrogenase0.15121.00163192
2-Hacid_dh_CD-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain020625.10187362
AdoHcyase_NADS-adenosyl-L-homocysteine hydrolase, NAD binding domain1.3E-072121.00217311
IlvNAcetohydroxy acid isomeroreductase, catalytic domain3.1E-092620.60219322
NAD_binding_2NAD binding domain of 6-phosphogluconate dehydrogenase3.8E-051321.00224312
TrkA_NTrkA-N domain0.000221121.70225268
ACTACT domain1.1E-123720.80553610
DUF3553Protein of unknown function (DUF3553)0.000151120.30564593

 624

2-Hacid_dh
NAD_binding_2
2-Hacid_dh_C
AdoHcyase_NAD
IlvN
NAD_binding_2
TrkA_N
ACT
DUF3553


References:

IlvN
9218783 The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution. EMBO J 1997;16:3405-3415.

NAD_binding_2

DUF3553

ACT
7719856 The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Nat Struct Biol 1995;2:69-76.
10222208 Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. J Mol Biol 1999;287:1023-1040.

2-Hacid_dh_C
9126843 Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution. J Mol Biol 1997;267:640-660.

2-Hacid_dh
9126843 Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution. J Mol Biol 1997;267:640-660.

AdoHcyase_NAD

TrkA_N
9478130 A novel family of predicted phosphoesterases includes Drosophila prune protein and bacterial RecJ exonuclease. Trends Biochem Sci 1998;23:17-19.
8412700 NAD+ binding to the Escherichia coli K(+)-uptake protein TrkA and sequence similarity between TrkA and domains of a family of dehydrogenases suggest a role for NAD+ in bacterial transport. Mol Microbiol 1993;9:533-543.
11292341 Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains. J Mol Biol 2001;307:1271-1292.