Protein Family Models for Protein (Select 738093754) - 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 4126633.

2-dehydropantoate 2-reductase N-terminal domain-containing protein

This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalysed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyses the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway [2]. ApbA and PanE are allelic [2]. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway [1]. [1]. 9488683. ApbA, the ketopantoate reductase enzyme of Salmonella typhimurium is required for the synthesis of thiamine via the alternative pyrimidine biosynthetic pathway. Frodyma ME, Downs D;. J Biol Chem 1998;273:5572-5576. [2]. 9721324. The panE gene, encoding ketopantoate reductase, maps at 10 minutes and is allelic to apbA in Salmonella typhimurium. Frodyma ME, Downs D;. J Bacteriol 1998;180:4757-4759. (from Pfam)

Date:: 2024-10-16

Family Accession:: NF014601.5
Method:: HMM

Select item 4123214.

NAD-binding protein

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)

GO Terms:

Biological Process:: potassium ion transport (GO:0006813)

Date:: 2024-10-16

Family Accession:: NF014325.5
Method:: HMM

Select item 4116115.

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 4082286.