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Iron-containing alcohol dehydrogenases-like, involved in the linear alkylbenzenesulfonate (LAS) degradation pathway. NAD-dependent iron-containing alcohol dehydrogenase-like. Proteins in this family are NAD-dependent alcohol dehydrogenases which are involved in the linear alkylbenzenesulfonate (LAS) degradation pathway. They catalyze the oxidation of beta-hydroxy CoA ester to beta-oxo CoA ester, which then be subject to CoA-dependent thiolysis to yield acetyl-CoA and 6-C8-SPC-CoA. The major laundry surfactant in worldwide use is commercial linear alkylbenzenesulfonate (LAS) which contains 20 congeners of linear alkanes (C10 to C13). LAS is fully biodegradable in oxic environments. Degradation involves microbial communities. Parvibaculum lavamentivorans DS-1T is a representative member of many heterotrophic, LAS-degrading communities, in which it catalyzes the first steps of LAS degradation. Strain DS-1T is a small heterotrophic bacterium able to omega-oxygenate the commercial surfactant linear alkylbenzenesulfonate (LAS) and shorten the side chain by beta-oxidation to yield sulfophenylcarboxylates (SPC). Parvibaculum lavamentivorans utilizes 3-C12-LAS as the sole carbon and energy source, and excretes largely 4-C6-SPC.
No pairwise interactions are available for this conserved domain.
Tips:  If you've navigated here from a protein, hovering over a position on the weblogo will display the corresponding protein position for that domain position. The histograms below the weblogo indicate mutations found on the domain. Red is for disease (OMIM) and blue is for SNPs. Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below. Range on the Protein: Protein ID Protein Position Domain Position: 
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