Protein Family Models for Protein (Select 736475588) - 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 4169522.

Acetohydroxy acid isomeroreductase, NADPH-binding domain

Acetohydroxy acid isomeroreductase catalyses the conversion of acetohydroxy acids into dihydroxy valerates. This reaction is the second in the synthetic pathway of the essential branched side chain amino acids valine and isoleucine. This N-terminal region of the enzyme carries the binding-site for NADPH. The active-site for enzymatic activity lies in the C-terminal part, IlvC, Pfam:PF01450. [1]. 9218783. The crystal structure of plant acetohydroxy acid isomeroreductase complexed with NADPH, two magnesium ions and a herbicidal transition state analog determined at 1.65 A resolution. Biou V, Dumas R, Cohen-Addad C, Douce R, Job D, Pebay-Peyroula E;. EMBO J 1997;16:3405-3415. [2]. 16322583. The crystal structure of a bacterial class II ketol-acid reductoisomerase: domain conservation and evolution. Tyagi R, Duquerroy S, Navaza J, Guddat LW, Duggleby RG;. Protein Sci. 2005;14:3089-3100. [3]. 19362563. Conformational changes in a plant ketol-acid reductoisomerase upon Mg(2+) and NADPH binding as revealed by two crystal structures. Leung EW, Guddat LW;. J Mol Biol. 2009;389:167-182. (from Pfam)

Date:: 2024-10-16

Family Accession:: NF019603.5
Method:: HMM

Select item 4154073.

NAD(P)-binding domain-containing protein

Date:: 2024-08-14

Family Accession:: NF015747.5
Method:: HMM

Select item 4143544.

NAD(P)-binding domain-containing protein

The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold. (from Pfam)

GO Terms:

Molecular Function:: NADP binding (GO:0050661)

Date:: 2024-08-14

Family Accession:: NF015411.5
Method:: HMM

Select item 4132565.

NAD(P)-dependent oxidoreductase

This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family Pfam:PF00389. [1]. 9126843. Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution. Dengler U, Niefind K, Kiess M, Schomburg D;. J Mol Biol 1997;267:640-660. (from Pfam)

GO Terms:

Molecular Function:: NAD binding (GO:0051287)

Date:: 2024-10-16

Family Accession:: NF014841.5
Method:: HMM

Select item 4116116.

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 4082287.