Protein Family Models for Protein (Select 828150122) - Protein Family Models

Select item 4311511.

prephenate dehydrogenase dimerization domain-containing protein

Members of this family are prephenate dehydrogenases EC:1.3.1.12 (PDHs) involved in tyrosine biosynthesis [1]. This is the C-terminal, helical dimerization domain of PDHs [1]. [1]. 31750992. Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain. Shabalin IG, Gritsunov A, Hou J, Slawek J, Miks CD, Cooper DR, Minor W, Christendat D;. FEBS J. 2020;287:2235-2255. (from Pfam)

Date:: 2024-10-16

Family Accession:: NF042869.3
Method:: HMM

Select item 4154072.

NAD(P)-binding domain-containing protein

Date:: 2024-08-14

Family Accession:: NF015747.5
Method:: HMM

Select item 4126113.

ACT domain-containing protein

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:: 2024-10-16

Family Accession:: NF013962.5
Method:: HMM

Select item 4116114.

prephenate dehydrogenase/arogenate dehydrogenase family protein

Members of this family are prephenate dehydrogenases (PDHs) EC:1.3.1.12 involved in tyrosine biosynthesis. This is the N-terminal nucleotide-binding domain of PDHs, which has a modified Rossmann nucleotide-binding fold with an extended beta-sheet sandwiched by three helices on each face [1]. [1]. 31750992. Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain. Shabalin IG, Gritsunov A, Hou J, Slawek J, Miks CD, Cooper DR, Minor W, Christendat D;. FEBS J. 2020;287:2235-2255. (from Pfam)

GO Terms:

Biological Process:: tyrosine biosynthetic process (GO:0006571)

Molecular Function:: prephenate dehydrogenase (NAD+) activity (GO:0008977)

Molecular Function:: arogenate dehydrogenase (NADP+) activity (GO:0033730)

Molecular Function:: NAD+ binding (GO:0070403)

Date:: 2024-10-16

Family Accession:: NF014234.5
Method:: HMM

Select item 4082285.