Component of the phenyllactate dehydratase complex FldABC that is involved in the fermentation of L-phenylalanine via a Stickland reaction. This complex catalyzes the reversible syn-dehydration of (R)-phenyllactate to (E)-cinnamate in two steps, a CoA-transfer from cinnamoyl-CoA to phenyllactate, catalyzed by FldA, followed by the dehydration of phenyllactyl-CoA to cinnamoyl-CoA, catalyzed by FldB and FldC. Requires the activator FldI to initiate catalysis. (R)-3-phenyllactoyl-CoA = (E)-cinnamoyl-CoA + H2O (R)-3-(4-hydroxyphenyl)lactoyl-CoA = (E)-4-coumaroyl-CoA + H2O (R)-3-(indol-3-yl)lactoyl-CoA = (E)-3-(indol-3-yl)acryloyl-CoA + H2O Appears to contain about 1 [4Fe-4S] cluster per heterodimer FldBC. No flavin coud be detected in the FldABC complex, and the addition of FAD, FMN or riboflavin to the dehydratase do not increase enzymatic activity. kcat is 1 sec(-1) (at pH 8 and 20 degrees Celsius). Values have been measured with the FldABC complex. Amino-acid degradation; L-phenylalanine degradation. Part of the heterotrimeric phenyllactate dehydratase complex FldABC, composed of (R)-phenyllactate CoA-transferase (FldA) and a heterodimeric (R)-phenyllactyl-CoA dehydratase (FldB and FldC). It seems that about 50 C-terminal amino acids have been lost by post-translational modification. Belongs to the FldB/FldC dehydratase alpha/beta subunit family.