{"metadata":{"accession":"PF01648","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR008278","hierarchy":null,"name":{"name":"4'-phosphopantetheinyl transferase superfamily","short":"ACPS"},"description":[{"text":"<p>Members of this family transfers the 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of [pfam:PF00550]. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP [[cite:PUB00002924]]. This superfamily consists of two subtypes: The ACPS type such as [swissprot:P24224] and the Sfp type such as [swissprot:P39135]. The structure of the Sfp type is known [[cite:PUB00011221]], which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Holo-(acyl-carrier-protein)_synthase","extract":"<p>In enzymology and molecular biology, a <b>holo-[acyl-carrier-protein] synthase</b> is an enzyme that catalyzes the chemical reaction:</p><dl><dd>CoA-[4'-phosphopantetheine] + apo-acyl carrier protein <span class=\"mwe-math-element mwe-math-element-inline\"><img src=\"https://wikimedia.org/api/rest_v1/media/math/render/svg/1c37b981df851b9e54e489e017b1481e37d418f3\" class=\"mwe-math-fallback-image-inline mw-invert skin-invert\" aria-hidden=\"true\" style=\"vertical-align:-0.338ex;width:2.324ex;height:1.843ex\" /></span> adenosine 3',5'-bisphosphate + holo-acyl carrier protein</dd></dl>","thumbnail":null}],"literature":{"PUB00011221":{"PMID":10581256,"ISBN":null,"volume":"18","issue":"23","year":1999,"title":"Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily.","URL":null,"raw_pages":"6823-31","medline_journal":"EMBO J","ISO_journal":"EMBO J.","authors":["Reuter K","Mofid MR","Marahiel MA","Ficner R."],"DOI_URL":"http://dx.doi.org/10.1093/emboj/18.23.6823"},"PUB00002924":{"PMID":7559576,"ISBN":null,"volume":"270","issue":"42","year":1995,"title":"Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase.","URL":null,"raw_pages":"24658-61","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Lambalot RH","Walsh CT."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.270.42.24658"},"PUB00019094":{"PMID":8939709,"ISBN":null,"volume":"3","issue":"11","year":1996,"title":"A new enzyme superfamily - the phosphopantetheinyl transferases.","URL":null,"raw_pages":"923-36","medline_journal":"Chem Biol","ISO_journal":"Chem. Biol.","authors":["Lambalot RH","Gehring AM","Flugel RS","Zuber P","LaCelle M","Marahiel MA","Reid R","Khosla C","Walsh CT."],"DOI_URL":"http://dx.doi.org/10.1016/S1074-5521(96)90181-7"}},"set_info":{"accession":"CL0670","name":"4PPT"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":348,"interactions":0,"matches":51752,"pathways":0,"proteins":51745,"proteomes":20259,"sets":1,"structural_models":{"alphafold":37610,"bfvd":2},"structures":107,"taxa":36900},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":143,"alignment:full":20469},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"5xu7","name":"Crystal structure of Escherichia coli holo-[acyl-carrier-protein] synthase (AcpS)"}}}