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NAD(P)-dependent oxidoreductase
This domain is found in fungi, plants, archaea and bacteria. (from Pfam)
NAD(P)-binding domain-containing protein
TrkA C-terminal domain-containing protein
This domain is often found next to the Pfam:PF02254 domain. The exact function of this domain is unknown. It has been suggested that it may bind an unidentified ligand [1]. The domain is predicted to adopt an all beta structure [1]. [1]. 11292341. Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains. Anantharaman V, Koonin EV, Aravind L;. J Mol Biol 2001;307:1271-1292. (from Pfam)
Shikimate / quinate 5-dehydrogenase
This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyses the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyses the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate. Discusses the pentafunctional AROM multi-domain protein, which possesses a shikimate 5-dehydrogenase enzyme. The AROM protein catalyses steps two to six in the shikimate pathway in many microbial eukaryotes. [1]. 7556173. The molecular biology of multidomain proteins. Selected examples. Hawkins AR, Lamb HK;. Eur J Biochem 1995;232:7-18. (from Pfam)
NAD-binding protein
This domain is found in a wide variety of proteins. These protein include potassium channels Swiss:P31069, phosphoesterases Swiss:Q59027, and various other transporters. This domain binds to NAD. Domain called KTN in figure 2. [1]. 9478130. A novel family of predicted phosphoesterases includes Drosophila prune protein and bacterial RecJ exonuclease. Aravind L, Koonin EV;. Trends Biochem Sci 1998;23:17-19. [2]. 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. Schlosser A, Hamann A, Bossemeyer D, Schneider E, Bakker EP;. Mol Microbiol 1993;9:533-543. Called TRKA-N domain. See alignment in figure 8a. [3]. 11292341. Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains. Anantharaman V, Koonin EV, Aravind L;. J Mol Biol 2001;307:1271-1292. (from Pfam)
Trk system potassium transport protein TrkA
Trk system potassium transport protein TrkA may regulate the transport activity of the constitutive potassium transport TrkG and TrkH systems; binds to NAD(+) and NADH
Trk system potassium transporter TrkA
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