Literature summary for 3.1.3.2 extracted from

Georgieva, D.; Greunke, K.; Genov, N.; Betzel, C.
3-D Model of the bee venom acid phosphatase: insights into allergenicity (2009), Biochem. Biophys. Res. Commun., 378, 711-715.

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Protein Variants

Protein Variants	Comment	Organism
additional information	3-D model of the Api m 3 tertiary structure: IgE epitopes and antigenic sites are predicted using programs based on the structure of known epitopes and analysis of the 3-D model. The model of Api m 3 reveals an active site similar to those of the histidine-type acid phosphatases with conservation of the catalytically important residues. The observed substitutions in the phosphate ion binding site suggest differences in the substrate specificity in comparison to other acid phosphatases	Apis mellifera

Organism

Organism	UniProt	Comment	Textmining
Apis mellifera	Q5BLY5	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Synonyms

Synonyms	Comment	Organism
acid phosphatase	-	Apis mellifera
Api m 3	-	Apis mellifera

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Release 2023.1 (January 2023)