Protein Family Models

This domain is found in fungi, plants, archaea and bacteria. (from Pfam)

Date:

2024-08-14

This family contains the NADP binding domain of saccharopine dehydrogenase. In some organisms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase. [1]. 11080625. Crystal structure of saccharopine reductase from Magnaporthe. grisea, an enzyme of the alpha-aminoadipate pathway of lysine. biosynthesis.. Johansson E, Steffens JJ, Lindqvist Y, Schneider G;. Structure Fold Des 2000;8:1037-1047.. [2]. 11354603. Lysine metabolism in higher plants.. Azevedo RA, Lea PJ;. Amino Acids 2001;20:261-279. (from Pfam)

Date:

2024-08-14

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:

2024-08-14

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:

2024-08-14

NAD(P)-binding protein may be the NAD(P)-binding component of a potassium uptake system similar to Trk system potassium uptake protein TrkA

Date:

2023-09-17