PKS_PPPhosphopantetheine attachment site |
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| SMART accession number: | SM00823 |
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| 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 (PUBMED:5321311). |
| Interpro abstract (IPR020806): | 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 [(PUBMED:5321311)]. The amino-terminal region of the ACP proteins is well defined and consists of alpha four 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 [(PUBMED:11825906)]. This entry represents the phosphopantetheine-binding domain from polyketide synthases. Polyketide synthases are large multidomain proteins involved in the synthesis of secondary metabolites [(PUBMED:15958783)]. |
| GO function: | phosphopantetheine binding (GO:0031177) |
| Family alignment: |
There are 6851 PKS_PP domains in 2659 proteins in SMART's nrdb database.
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- Evolution (species in which this domain is found)
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- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
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