F57E68EB3E648D10E7F381D0609A22F69B1DEC1963FBFF3B2700727606BE976B3A2A071A41AAD70F788F7C0EBF273EC9

Adenylyltransferase activity is inhibited by the inhibitory helix present at the N-terminus: Glu-252 binds ATP and competes with ATP-binding at Arg-391, thereby preventing adenylyltransferase activity. Activation dissociates ATP-binding from Glu-252, allowing ordered binding of the entire ATP moiety with the alpha-phosphate in an orientation that is productive for accepting an incoming target hydroxyl side chain (By similarity).

Source:http://purl.uniprot.org/SHA-384/F57E68EB3E648D10E7F381D0609A22F69B1DEC1963FBFF3B2700727606BE976B3A2A071A41AAD70F788F7C0EBF273EC9

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Predicate	Object
rdf:type	uniprot:Enzyme_Regulation_Annotation
rdfs:comment	Adenylyltransferase activity is inhibited by the inhibitory helix present at the N-terminus: Glu-252 binds ATP and competes with ATP-binding at Arg-391, thereby preventing adenylyltransferase activity. Activation dissociates ATP-binding from Glu-252, allowing ordered binding of the entire ATP moiety with the alpha-phosphate in an orientation that is productive for accepting an incoming target hydroxyl side chain (By similarity).