Literature summary extracted from

Xiang, T.; Liu, Q.; Deacon, A.M.; Koshy, M.; Kriksunov, I.A.; Lei, X.G.; Hao, Q.; Thiel, D.J.
Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine (2004), J. Mol. Biol., 339, 437-445.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.1.3.8	hanging-drop vapour diffusion method at 22°C, crystal structure determined at 1.5 A resolution. The crystal structure clearly shows a partially occupied phosphohistidine residue, the transient reaction intermediate of the enzyme, at the active site	Aspergillus fumigatus
3.1.3.26	hanging-drop vapour diffusion method at 22°C, crystal structure determined at 1.5 A resolution. The crystal structure clearly shows a partially occupied phosphohistidine residue, the transient reaction intermediate of the enzyme, at the active site	Aspergillus fumigatus

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.1.3.8	Aspergillus fumigatus	-	The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.	-
3.1.3.26	Aspergillus fumigatus	-	The enzyme may be a 3-phytase (EC 3.1.3.8), or a 4-phytase (synonym 6-phytase, EC 3.1.3.26). The product of the hydrolysis of myo-inositol hexakisphosphate to 1D-myo-inositol 1,2,4,5,6-pentakisphosphate or alternatively 1D-myo-inositol 1,2,3,5,6-pentakisphosphate has not been identified.	-

Posttranslational Modification

EC Number	Posttranslational Modification	Comment	Organism
3.1.3.8	glycoprotein	six predicted N-glycosylation sites are observed to be glycosylated from the experimental electron density	Aspergillus fumigatus
3.1.3.26	glycoprotein	six predicted N-glycosylation sites are observed to be glycosylated from the experimental electron density	Aspergillus fumigatus

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Release 2023.1 (January 2023)