Transferases;
Transferring phosphorus-containing groups;
Nucleotidyltransferases
BRITE hierarchy

[protein] L-serine/L-threonine/L-tyrosine adenylyltransferase

(1) ATP + a [protein]-L-serine = diphosphate + a [protein]-O-(5'-adenylyl)-L-serine;
(1) ATP + a [protein]-L-threonine = diphosphate + a [protein]-O-(5'-adenylyl)-L-threonine;
(1) ATP + a [protein]-L-tyrosine = diphosphate + a [protein]-O-(5'-adenylyl)-L-tyrosine

ATP [CPD:C00002];
[protein]-L-serine [CPD:C02189];
[protein]-L-threonine [CPD:C19803];
[protein]-L-tyrosine [CPD:C00585]

The enzyme, commonly referred to as AMPylase, transfers an adenylyl (adenosine 5'-phosphate) group from ATP to L-serine, L-threonine, and L-tyrosine residues in its target protein substrates. AMPylation is found in both prokaryotes and eukaryotes. In bacteria AMPylases are abundant enzymes that either regulate the function of endogenous bacterial proteins or are translocated into host cells to hijack host cell signalling processes. Metazoans AMPylases are either enzymes containing a conserved Fic domain that primarily modify the ER-resident chaperone BiP, or mitochondrial selenocysteine-containing proteins (SelO) involved in redox signalling.

EC 2.7.7.108 created 2022