$small{D}$-Phenylglycine aminotransferase ($small{D}$-PhgAT) from Pseudomonas stutzeri ST-201 is useful for enzymatic synthesis of enantiomerically pure $small{D}$-phenylglycine. However, its low protein solubility prevents its application at high substrate concentration. With an aim to increase the protein solubility, the N-terminus of $small{D}$-PhgAT was genetically fused with short peptides ($A_1$ ${alpha}$-helix, $A_2$ ${alpha}$-helix, and ALAL, which is a hybrid of $A_1$ and $A_2$) from a ferredoxin enzyme of a halophilic archaeon, Halobacterium salinarum. The fused enzymes $A_1$-$small{D}$-PhgAT, $A_2$-$small{D}$-PhgAT, and ALAL-$small{D}$-PhgAT displayed a reduced pI and increased in solubility by 6.1-, 5.3-, and 8.1- fold in TEMP (pH 7.6) storage, respectively, and 5-, 4.5-, and 5.9-fold in CAPSO (pH 9.5) reaction buffers, respectively, compared with the wild-type enzyme (WT-$small{D}$-PhgAT). In addition, all the fused $small{D}$-PhgAT displayed higher enzymatic reaction rates than the WT-DPhgAT at all concentrations of L-glutamate monosodium salt used. The highest rate, $23.82{pm}1.47$ mM/h, was that obtained from having ALAL-$small{D}$-PhgAT reacted with 1,500 mM of the substrate. Moreover, the halophilic fusion significantly increased the tolerance of $small{D}$-PhgAT in the presence of NaCl and KCl, being slightly in favor of KCl, where under the same condition at 3.5 M NaCl or KCl all halophilic-fused variants showed higher activity than WT-$small{D}$-PhgAT.