Protein Family Models

This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model. (from Pfam)

Date:

2024-08-14

This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95 Swiss:P08328, which is inhibited by serine [1]. Aspartokinase EC:2.7.2.4 Swiss:P53553, which is regulated by lysine. Acetolactate synthase small regulatory subunit Swiss:P00894, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1 Swiss:P00439, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51 Swiss:P21203. formyltetrahydrofolate deformylase EC:3.5.1.10, Swiss:P37051, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5 Swiss:P11585 [1]. 7719856. The allosteric ligand site in the Vmax-type cooperative enzyme. phosphoglycerate dehydrogenase.. Schuller DJ, Grant GA, Banaszak LJ;. Nat Struct Biol 1995;2:69-76.. Definition of the domain. [2]. 10222208. Gleaning non-trivial structural, functional and evolutionary. information about proteins by iterative database searches.. Aravind L, Koonin EV;. J Mol Biol 1999;287:1023-1040. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

homoserine dehydrogenase catalyzes the conversion from L-homoserine and NAD(P)(+) to L-aspartate 4-semialdehyde and NAD(P)H

Date:

2023-03-03

Catalyzes the formation of L-aspartate 4-semialdehyde from L-homoserine

Date:

2021-08-24