*2.3. D-Structural Modeling*

The programs for 3D structural modeling automatically selected template structures mostly from fungal lipases as shown in Table S1 (PDBs: 6A0w, 6qpr, 4jei, 3o0d, 6unv, 4tgl, 3tgl). All models presented the typical α/β-hydrolase fold, with mostly parallel β-sheets, flanked on both sides by α-helixes. The highly conserved catalytic triad (serine, aspartic/glutamic acid and histidine) and the oxyanionic hole were well orientated in the space. The α/β hydrolase fold is one of the most thriving architectures in proteins across kingdoms, providing the skeleton for diverse enzymes [19] as well as an emerging class of non-catalytic but functionally important receptors [20]. Some of the predicted structures were very similar with the typical lipase motifs and are formed by one domain, but some other possesses an extra-transmembrane domain which could be quite bulky (Lip\_4551 displays 9 helices against 4 for Lip\_3928). Few membrane-bound lipases over intracellular or extracellular counterparts were studied. Recently the catalytic behavior of a membraneassociated lipolytic enzyme (MBL-Enzyme) from the microalgae *Nannochloropsis oceanica* was investigated by Savvidou et al. [21].
