Aminotransferase that acts exclusively on beta-amino acids and exhibits a broad substrate range in vitro, accepting meta-, para- and, to a lesser extent, ortho-substituted beta-phenylalanine derivatives as amino donors, and 2-oxoglutarate or pyruvate as amino acceptors. Is highly enantioselective toward (S)-beta-phenylalanine (is not active with (R)-beta-phenylalanine) and derivatives with different substituents on the phenyl ring, allowing the kinetic resolution of various racemic beta-amino acids to yield (R)-beta-amino acids with >95% enantiomeric excess (ee). Highly prefers aromatic beta-amino acids over aliphatic beta-amino acids; cannot use beta-alanine or beta-glutamate as substrate. Is likely involved in the beta-phenylalanine degradation pathway that allows V.paradoxus strain CBF3 to use beta-phenylalanine as a sole nitrogen source. (S)-3-amino-3-phenylpropanoate + 2-oxoglutarate = 3-oxo-3-phenylpropanoate + L-glutamate (S)-3-amino-3-phenylpropanoate + pyruvate = 3-oxo-3-phenylpropanoate + L-alanine Binds 1 pyridoxal phosphate per subunit. Is inhibited by 2-aminooxyacetate (AOA), a mimic of beta-alanine and a known inhibitor of aminotransferases. kcat is around 11 sec(-1) with (S)-beta-phenylalanine and 2-oxoglutarate as substrates. Has high activity over a broad pH range (4 to 11.2). Optimum temperature is 55 degrees Celsius. Displays a 2-fold higher activity at 55 degrees Celsius than at 30 degrees Celsius. Homodimer. Is an attractive template for future beta-aminotransferase-engineering efforts toward the synthesis of enantiomerically pure beta-amino acids. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.