Protein Family Models

This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

This family now also contains the lysine 2-oxoglutarate reductases. [1]. 11354603. Lysine metabolism in higher plants. Azevedo RA, Lea PJ;. Amino Acids 2001;20:261-279. (from Pfam)

Date:

2024-10-16

This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family Pfam:PF00389. [1]. 9126843. Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution. Dengler U, Niefind K, Kiess M, Schomburg D;. J Mol Biol 1997;267:640-660. (from Pfam)

Date:

2024-10-16

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)

Date:

2024-10-16

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)

Date:

2024-10-16

This family now also contains the lysine 2-oxoglutarate reductases. [1]. 11354603. Lysine metabolism in higher plants. Azevedo RA, Lea PJ;. Amino Acids 2001;20:261-279. (from Pfam)

Date:

2024-10-16

This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)

Date:

2024-10-16