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<i>p</i>-Coumaric acid is a commercially available phenolcarboxylic acid with a great number of important applications in the nutraceutical, pharmaceutical, material and chemical industries. <i>p</i>-Coumaric acid has been biosynthesized in some engineered microbes, but the potential of the plant CYP450-involved biosynthetic route has not investigated in <i>Escherichia coli</i>. In the present study, a novel <i>trans</i>-cinnamic acid 4-hydroxylase (C4H) encoding the <i>Lau</i>C4H gene was isolated from <i>Lycoris aurea</i> (L&#8217; H&#233;r.) Herb via rapid amplification of cDNA ends. Then, <i>N</i>-terminal 28 amino acids of <i>Lau</i>C4H were characterized, for the subcellular localization, at the endoplasmic reticulum membrane in protoplasts of <i>Arabidopsis thaliana</i>. In <i>E. coli</i>, <i>Lau</i>C4H without the <i>N</i>-terminal membrane anchor region was functionally expressed when fused with the redox partner of <i>A. thaliana</i> cytochrome P450 enzyme (CYP450), and was verified to catalyze the <i>trans</i>-cinnamic acid to <i>p</i>-coumaric acid transformation by whole-cell bioconversion, HPLC detection and LC-MS analysis as well. Further, with phenylalanine ammonia-lyase 1 of <i>A. thaliana</i>, <i>p</i>-coumaric acid was de novo biosynthesized from glucose as the sole carbon source via the phenylalanine route in the recombinant <i>E. coli</i> cells. By regulating the level of intracellular NADPH, the production of <i>p</i>-coumaric acid was dramatically improved by 9.18-fold, and achieved with a titer of 156.09 &#956;M in shake flasks. The recombinant cells harboring functional <i>Lau</i>C4H afforded a promising chassis for biological production of <i>p</i>-coumaric acid, even other derivatives, via a plant CYP450-involved pathway.