This C-terminal domain is found in prokaryotic acetaldehyde dehydrogenases, it adopts a structure consisting of an alpha-beta-alpha-beta(3) core, which mediates dimerisation of the protein [1].
The acetaldehyde dehydrogenase family of bacterial enzymes catalyses the formation of acetyl-CoA from acetaldehyde in the 3-hydroxyphenylpropinoate degradation pathway. It occurs as a late step in the meta-cleavage pathways of a variety of compounds, including catechol, biphenyl, toluene, salicylate [2].
Manjasetty BA, Powlowski J, Vrielink A.
Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate.
Proc. Natl. Acad. Sci. U.S.A. 100 6992-7 2003
[PubMed: 12764229] http://dx.doi.org/10.1073/pnas.1236794100
2.
Shingler V, Powlowski J, Marklund U.
Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600.
J. Bacteriol. 174 711-24 1992
[PubMed: 1732207] http://jb.asm.org/cgi/content/abstract/174/3/711
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