Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds (Probable). It is spontaneously inactivated by its substrate and reactivated by EutA (By similarity). May play a role in bacterial microcompartment (BMC) assembly or maintenance (Probable). Directly targeted to the BMC (PubMed:22428024, PubMed:27063436, PubMed:27450681). Expression of the eut operon allows this bacteria to use ethanolamine (EA) as a carbon, nitrogen and energy source. It relies on cobalamin (vitamin B12) both as a cofactor for the ethanolamine ammonia-lyase activity and to induce the operon. EA enhances bacterial survival in macrophages in a concentration-dependent manner, suggesting it is an important nutrient during infection (PubMed:29531136). ethanolamine = acetaldehyde + NH4(+) Binds between the large and small subunits. Amine and polyamine degradation; ethanolamine degradation. The basic unit is a heterodimer which dimerizes to form tetramers (PubMed:1550360). The heterotetramers trimerize; 6 large subunits form a core ring with 6 small subunits projecting outwards (Probable). Interacts with EutS, which targets it to the interior of the BMC (PubMed:22428024, PubMed:27063436, PubMed:27450681). Probably located inside the BMC (Probable). Has been suggested to be on the BMC exterior. Part of the 17-gene eut operon transcribed from a single promoter, induced by ethanolamine and adenosylcobalamin (AdoCbl, vitamin B12). The first 19 residues target foreign proteins (tested with eGFP, mCherry and lacZ) to the BMC both in situ and in E.coli. The cargo is only detected by Western blot in broken shells, strongly suggesting this protein is normally found inside the BMC and not on its exterior. No aerobic growth on ethanolamine (EA) supplemented with cobalamin (vitamin B12) (PubMed:10464203, PubMed:2656649). A non-polar deletion mutant does not grow on EA between pH 5.5 and pH 8.5 (PubMed:16585748). A deletion allows growth on acetate, suggesting BMC assembly or maintenance is impaired (PubMed:23585538). Artificial BMCs can be made in E.coli by expressing eutK, eutL, eutM, eutN, eutS (eutSMNLK) or eutS alone. Cargo proteins can be targeted to them using the first 19 residues of this protein. Beta-galactosidase (lacZ) was active within the BMC, showing the BMC allows passage of substrate into the interior. This can lead to the development of tailored BMCs for specific metabolic reactions. Belongs to the EutC family.