Salvianolic acids (SA), including rosmarinic acid (RA), danshensu (DSS), and salvianolic acid B (SAB), are widely found in Lamiaceae and Boraginaceae families and have significant medicinal properties. Previous studies have identified 4-coumaroyl-CoA and 4-hydroxyphenylacetic acid (4-HPL) as common substrates for SA biosynthesis, catalyzed by rosmarinic acid synthase (RAS) and cytochrome P450 98A (CYP98A) subfamily enzymes. However, recent studies have revealed that various acyl donors and acceptors, including DSS and its ester-forming products, are also present in SA-rich plants, suggesting that the previous understanding of SA biosynthesis is incomplete. This study used *Salvia miltiorrhiza*, a rich source of SA, to investigate the diversity of SA biosynthesis. The research identified multiple acyl donors and acceptors, including DSS, catalyzed by SmRAS to form precursors of RA. Two SmCYP98A family members, SmCYP98A14 and SmCYP98A75, were responsible for the meta-hydroxylation of these precursors at different positions. SmCYP98A75 preferentially catalyzed C-3' hydroxylation, while SmCYP98A14 preferentially catalyzed C-3 hydroxylation. Notably, SmCYP98A75 was verified as the first enzyme involved in DSS formation. Knockout of both enzymes using CRISPR/Cas9 resulted in a significant decrease in SA accumulation, while overexpression of these enzymes increased SA content. This study provides new insights into the diversity of SA biosynthesis in SA-abundant species and highlights the versatility of CYP98A enzymes in meta-hydroxylation reactions. Additionally, CYP98A enzymes are identified as ideal targets for metabolic engineering to enhance SA content.Salvianolic acids (SA), including rosmarinic acid (RA), danshensu (DSS), and salvianolic acid B (SAB), are widely found in Lamiaceae and Boraginaceae families and have significant medicinal properties. Previous studies have identified 4-coumaroyl-CoA and 4-hydroxyphenylacetic acid (4-HPL) as common substrates for SA biosynthesis, catalyzed by rosmarinic acid synthase (RAS) and cytochrome P450 98A (CYP98A) subfamily enzymes. However, recent studies have revealed that various acyl donors and acceptors, including DSS and its ester-forming products, are also present in SA-rich plants, suggesting that the previous understanding of SA biosynthesis is incomplete. This study used *Salvia miltiorrhiza*, a rich source of SA, to investigate the diversity of SA biosynthesis. The research identified multiple acyl donors and acceptors, including DSS, catalyzed by SmRAS to form precursors of RA. Two SmCYP98A family members, SmCYP98A14 and SmCYP98A75, were responsible for the meta-hydroxylation of these precursors at different positions. SmCYP98A75 preferentially catalyzed C-3' hydroxylation, while SmCYP98A14 preferentially catalyzed C-3 hydroxylation. Notably, SmCYP98A75 was verified as the first enzyme involved in DSS formation. Knockout of both enzymes using CRISPR/Cas9 resulted in a significant decrease in SA accumulation, while overexpression of these enzymes increased SA content. This study provides new insights into the diversity of SA biosynthesis in SA-abundant species and highlights the versatility of CYP98A enzymes in meta-hydroxylation reactions. Additionally, CYP98A enzymes are identified as ideal targets for metabolic engineering to enhance SA content.