| Description | 4-hydroxy 2-ketovalerate aldolase (also known as 4-hydroxy-2-ketovalerate aldolase and 4-hydroxy-2-oxopentanoate aldolase (HOA)) converts 4-hydroxy-2-oxopentanoate to acetaldehyde and pyruvate, the penultimate step in the meta-cleavage pathway for the degradation of phenols, cresols and catechol. Acetaldehyde is then converted by acetaldehyde dehydrogenase (acylating) (DmpF; ) to acetyl-CoA. The two enzymes are tightly associated. This family includes the Escherichia coli MhpE aldolase [ ], the Pseudomonas DmpG aldolase, and the Burkholderia xenovorans BphI pyruvate aldolase []. In Pseudomonas, the DmpG aldolase tightly associates with a dehydrogenase (DmpF) and is inactive without it []. HOA has a canonical TIM-barrel fold with a C-terminal extension that forms a funnel leading to the active site []. This family belongs to the DRE-TIM metallolyase superfamily.DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core β(8)-α(8) motif with the eight parallel β strands forming an enclosed barrel surrounded by eight α helices. The domain has a catalytic centre containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name 'DRE-TIM' [ ].This entry represents the N-terminal catalytic TIM barrel domain. | Name | 4-hydroxy-2-oxovalerate aldolase, N-terminal catalytic TIM barrel domain |
| Short Name | DRE_TIM_HOA | Type | Domain |
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