UniProt functional annotation for P11454

UniProt code: P11454.

Organism: Escherichia coli (strain K12).
Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.
 
Function: Activates the carboxylate group of L-serine via ATP-dependent PPi exchange reactions to the aminoacyladenylate, preparing that molecule for the final stages of enterobactin synthesis. Holo-EntF acts as the catalyst for the formation of the three amide and three ester bonds present in the cyclic (2,3-dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE).
 
Catalytic activity: Reaction=ATP + L-serine = diphosphate + L-seryl-5'-AMP; Xref=Rhea:RHEA:28570, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:61231;
Cofactor: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Note=Binds 1 phosphopantetheine covalently.;
Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Subunit: EntB, EntD, EntE, and EntF form a multienzyme complex called enterobactin synthase. EntF acts as a catalytic monomer.
Induction: Transcriptionally regulated by iron and the fur protein.
Ptm: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-EntF by EntD. Holo-EntF so formed is then acylated with seryl- AMP.
Similarity: Belongs to the ATP-dependent AMP-binding enzyme family. EntF subfamily. {ECO:0000305}.
Sequence caution: Sequence=AAB40785.1; Type=Erroneous initiation; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.