Protein Domain : Polyketide synthase, phosphopantetheine-binding domain IPR020806

Type  Domain
Description  Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups [ ].The amino-terminal region of the ACP proteins is well defined and consists of four α helices arranged in a right-handed bundle held together by interhelical hydrophobic interactions. The Asp-Ser-Leu (DSL) motif is conserved in all of the ACP sequences, and the 4'-PP prosthetic group is covalently linked via a phosphodiester bond to the serine residue. The DSL sequence is present at the amino terminus of helix II, a domain of the protein referred to as the recognition helix and which is responsible for the interaction of ACPs with the enzymes of type II fatty acid synthesis [ ].This entry represents the phosphopantetheine-binding domain from polyketide synthases. Polyketide synthases are large multidomain proteins involved in the synthesis of secondary metabolites [ ].
Short Name  PKS_PP-bd

0 Child Features

0 Gene Families

437 Genes

1 Ontology Annotations

1 Parent Features

13 Publications

USDA
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