Plays a key role in glycolysis by catalyzing the cleavage of fructose 1,6-bisphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate (PubMed:26289816). Independently of its catalytic activity, connects the actin filaments, and thus the actomyosin motor, to cell surface adhesins of the thrombospondin-related anonymous protein (TRAP), the erythrocyte binding ligand (EBL) and reticulocyte binding homolog (RH) protein families; this interaction is probably involved in transducing the motor force across the parasite surface required for sporozoite and ookinete gliding motility and merozoite invasion (PubMed:22991428, PubMed:25261592) (Probable). Stimulates actin polymerisation (PubMed:25261592). beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate The cytoplasmic tail of TRAP and probably other adhesins acts as a competitive inhibitor as the binding sites of the glycolytic substrate fructose 1,6-bisphosphate and TRAP partially overlap. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Homotetramer (PubMed:26289816). Interacts with TRAP (via cytoplasmic domain); the interaction prevents substrate binding and thereby inhibits aldolase activity (PubMed:26289816, PubMed:16321976) (Probable). Interacts with MTRAP (via cytoplasmic domain); MTRAP phosphorylation may increase the binding to FBPA (PubMed:16321976). Interact with RH1 (via cytoplasmic domain) (PubMed:22991428, PubMed:27607074). Interacts with RH2b (via cytoplasmic domain) (PubMed:22991428, PubMed:27607074). Interacts with RH4 (via cytoplasmic domain) (PubMed:22991428, PubMed:27607074). Interacts with AMA1 (via cytoplasmic domain); the interaction is weak, however it may be increased upon AMA1 phosphorylation (PubMed:27607074). Interacts with EBA140 (via cytoplasmic domain); the interaction is weak (PubMed:27607074). Interacts with EBA175 (via cytoplasmic domain); the interaction is weak (PubMed:27607074). Interacts with EBA181 (via cytoplasmic domain); the interaction is weak (PubMed:27607074). Interacts with G-actin and F-actin (PubMed:25261592). May interact with ACT2/actin II; the interaction inhibits FBPA catalytic activity (By similarity). Interacts with human SLC4A1/band 3 (via N-terminus); the interaction inhibits FBPA catalytic activity (By similarity). Expressed during parasite asexual blood stages, including in schizonts (at protein level). Belongs to the class I fructose-bisphosphate aldolase family.