"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"PF01648"	"{'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}"	"{}"	"[{'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}]"	""	""	""	"IPR008278"	False	False	False	"{'PUB00011221': {'PMID': 10581256, 'ISBN': None, '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': None, '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': None, 'volume': '270', 'issue': '42', 'year': 1995, 'title': 'Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase.', 'URL': None, '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': None, 'volume': '3', 'issue': '11', 'year': 1996, 'title': 'A new enzyme superfamily - the phosphopantetheinyl transferases.', 'URL': None, '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'}}"	""	"{'name': ""4'-phosphopantetheinyl transferase superfamily"", 'short': 'ACPS'}"	""	"{'accession': '5xu7', 'name': 'Crystal structure of Escherichia coli holo-[acyl-carrier-protein] synthase (AcpS)'}"	"{'accession': 'CL0670', 'name': '4PPT'}"	"pfam"	"domain"	"[{'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': None}]"