<![CDATA[Fruit aroma arises from volatile esters synthesized by alcohol acyltransferase (AAT) of the BAHD family. This study analyzes AATs from Citrus sinensis, Vitis vinifera, Malus domestica, and Fragaria × ananassa through sequence alignment, secondary structure prediction, 3D modeling, and docking with acetyl-CoA. Secondary structure prediction shows conserved α-helices and β-sheets forming the characteristic α/β fold, with loops providing interspecies variation. all AATs retain the HXXXD motif and DFGWG/NFGWG variants with ~450 residues. Docking reveals a consistent acetyl-CoA orientation but species-specific interactions: polar/charged residues (Arg, Ser, His, Gln/Asn) form hydrogen and electrostatic bonds, whereas aromatic/aliphatic residues (Phe, Ile, Met) provide hydrophobic stabilization. Malus domestica exhibits the strongest polar network (6 H-bonds; ≈ −7.8 kcal·mol⁻¹), whereas Citrus sinensis relies more on hydrophobic contacts (≈ −6.9 kcal·mol⁻¹). These findings indicate that a conserved structural framework preserves the core catalytic mechanism of AATs while species-specific active-site microarchitecture modulates substrate affinity and selectivity, likely contributing to differences in fruit volatile ester profiles and offering candidate residues for targeted functional validation and aroma improvement.]]>
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