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DmpG-like communication domain
This domain is found towards the C-terminal region of various aldolase enzymes. It consists of five alpha-helices, four of which form an antiparallel helical bundle that plugs the C-terminus of the N-terminal TIM barrel domain [1]. The communication domain is thought to play an important role in the heterodimerisation of the enzyme [1]. [1]. 12764229. Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate. Manjasetty BA, Powlowski J, Vrielink A;. Proc Natl Acad Sci U S A 2003;100:6992-6997. (from Pfam)
HMGL-like
This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase. (from Pfam)
4-hydroxy-2-oxovalerate aldolase
4-hydroxy-2-oxovalerate aldolase 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
Members of this protein family are 4-hydroxy-2-oxovalerate aldolase, also called 4-hydroxy-2-ketovalerate aldolase and 2-oxo-4-hydroxypentanoate aldolase. This enzyme, part of the pathway for the meta-cleavage of catechol, produces pyruvate and acetaldehyde. Acetaldehyde is then converted by acetaldehyde dehydrogenase (acylating) (DmpF; EC 1.2.1.10) to acetyl-CoA. The two enzymes are tightly associated.
4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase,
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