3‐Deoxy‐d‐arabino‐heptulosonate 7‐phosphate synthase (DAHP synthase) encoded by aroF is the first enzyme of the shikimate pathway. In the present study, an AroF variant with a deficiency in residue Ile11 (named AroF*) was shown to be insensitive to l‐tyrosine. According to three‐dimensional structure analysis, nine AroF variants were constructed with truncation of different N‐terminal fragments, and overexpression of the variants AroFΔ(1–9), AroFΔ(1–10), AroFΔ(1–12) and, in particular, AroFΔ(1–11) significantly increased the accumulation of l‐phenylalanine (l‐Phe). However, the AroG and AroH variants with similar truncations of the N‐terminal fragments decreased the production of l‐Phe. By co‐overexpressing AroFΔ(1–11) and PheAfbr, the production of l‐Phe was increased from 2.36 ± 0.07 g L−1 (co‐overexpression of the wild‐type AroF and PheAfbr) to 4.29 ± 0.06 g L−1. The novel variant AroFΔ(1–11) showed great potential for the production of aromatic amino acids and their derivatives.