Protein Family Models

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:

2024-10-16

This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1 [1-3]. [1]. 11713534. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Lake MW, Wuebbens MM, Rajagopalan KV, Schindelin H;. Nature. 2001;414:325-329. [2]. 15660128. Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. Lois LM, Lima CD;. EMBO J. 2005;24:439-451. [3]. 18662542. Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes. Lee I, Schindelin H;. Cell. 2008;134:268-278. (from Pfam)

Date:

2024-10-16

HesA/MoeB/ThiF family protein is an E1-like enzyme containing an NAD/FAD-binding fold that is involved in molybdopterin and thiamine biosynthesis

Date:

2024-09-03