Protein Family Models

3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidised to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure [1]. [1]. 16126223. Crystal structure of novel NADP-dependent 3-hydroxyisobutyrate. dehydrogenase from Thermus thermophilus HB8.. Lokanath NK, Ohshima N, Takio K, Shiromizu I, Kuroishi C,. Okazaki N, Kuramitsu S, Yokoyama S, Miyano M, Kunishima N;. J Mol Biol. 2005;352:905-917. (from Pfam)

Date:

2024-08-14

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:

2024-08-14

Date:

2024-08-14

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

Date:

2024-08-14

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)

Date:

2024-08-14

3-hydroxyisobutyrate dehydrogenase is an enzyme that catalyzes the NAD+-dependent oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde of the valine catabolism pathway. In Pseudomonas aeruginosa, 3-hydroxyisobutyrate dehydrogenase (mmsB) is co-induced with methylmalonate-semialdehyde dehydrogenase (mmsA) when grown on medium containing valine as the sole carbon source. The positive transcriptional regulator of this operon (mmsR) is located upstream of these genes and has been identified as a member of the XylS/AraC family of transcriptional regulators [1]. 3-hydroxyisobutyrate dehydrogenase shares high sequence homology to the characterized 3-hydroxyisobutyrate dehydrogenase from rat liver [2] with conservation of proposed NAD+ binding residues at the N-terminus (G-8,10,13,24 and D-31). This enzyme belongs to the 3-hydroxyacid dehydrogenase family, sharing a common evolutionary origin and enzymatic mechanism with 6-phosphogluconate [3]. HIBADH exhibits sequence similarity to the NAD binding domain of 6-phosphogluconate dehydrogenase above trusted (PF03446).

Gene:

mmsB

Date:

2024-06-27