3.7.1.4	evolution	C-C-cleaving hydrolases catalyzing reactions similar to the reaction carried out by phloretin hydrolase belong to the alpha/beta-hydrolase fold superfamily, but since the phloretin hydrolase sequence of Eubacterium ramulus has no sequence similarity to other C-C-cleaving hydrolases and also does not contain the conserved sequence motif GXSXG, it can be assumed that this enzyme belongs to another enzyme family. The sequences of phloretin hydrolase, Phy, and 2,4-diacetylphloroglucinol hydrolase, PhlG, show no similarities to any other protein sequences with known functions deposited in database	-, 654284	
3.7.1.4	metabolism	the enzyme is involved in the metabolic pathway of icariin, epimedin A, B, and C, and f baohuoside I in intestinal flora and enzyme of rats, detailed overview	-, 732550	
3.7.1.4	additional information	comparison of the enzyme phloretin hydrolase Phy from Eubacterium ramulus with the diacetyl phloroglucinol hydrolase (Phlg) from Pseudomonas fluorescens, which catalyses a similar, hydrolytic, de-acylation of its substrate, homology modeling of Phy based on the structure of Phlg, PDB ID 3HWP	735304	
3.7.1.4	physiological function	phloretin hydrolase catalyzes the hydrolytic C-C cleavage of phloretin to phloroglucinol and 3-(4-hydroxyphenyl) propionic acid during flavonoid degradation in Eubacterium ramulus	-, 654284	
3.7.1.4	physiological function	the enzyme catalyses the degradation of plant-derived dihydrochalcone phloretin	735304	
3.7.1.4	physiological function	the enzyme plays a major role in the deglycosylation of daidzin	-, 732550