| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.7.-.- |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.-.-.- |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/enzyme/2.7.8.- |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2000/01/rdf-schema#subClassOf | http://purl.uniprot.org/core/Enzyme |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2000/01/rdf-schema#comment | "Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14."xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2000/01/rdf-schema#comment | "All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active."xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2000/01/rdf-schema#comment | "The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain."xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase system (EC 2.3.1.85) and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes."xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2004/02/skos/core#prefLabel | "holo-[acyl-carrier-protein] synthase"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/8939709 |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/11489886 |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12815048 |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/4561013 |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/4872726 |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9667867 |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2004/02/skos/core#altLabel | "holo-ACP synthase"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2004/02/skos/core#altLabel | "4'-phosphopantetheinyl transferase"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2004/02/skos/core#altLabel | "L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2004/02/skos/core#altLabel | "acyl carrier protein synthase"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2004/02/skos/core#altLabel | "ACPS"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2004/02/skos/core#altLabel | "PPTase"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2004/02/skos/core#altLabel | "P-pant transferase"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2004/02/skos/core#altLabel | "acyl carrier protein synthetase"xsd:string |
| http://purl.uniprot.org/enzyme/2.7.8.7 | http://www.w3.org/2004/02/skos/core#altLabel | "holo-ACP synthetase"xsd:string |