Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
A [auth B]d3ne3b_ Alpha and beta proteins (a+b) 4'-phosphopantetheinyl transferase 4'-phosphopantetheinyl transferase automated matches automated matches (Mycobacterium tuberculosis ) [TaxId: 1773 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
A [auth B]SCOP2B Superfamily4'-phosphopantetheinyl transferase8083766 3000948 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth B]ACPS_1e3ne3B1 A: a+b three layersX: Bacillus chorismate mutase-likeH: 4'-phosphopantetheinyl transferase (From Topology)T: 4'-phosphopantetheinyl transferaseF: ACPS_1ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A [auth B]3.90.470.20 Alpha Beta Alpha-Beta Complex Ribosomal Protein L22 Chain ACATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A [auth B]PF016484'-phosphopantetheinyl transferase superfamily (ACPS)4'-phosphopantetheinyl transferase superfamilyMembers 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 ...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 [1]. This superfamily consists of two subtypes: The ACPS type such as Swiss:P24224 and the Sfp type such as Swiss:P39135. The structure of the Sfp type is known [3], which shows the active site accommodates a magnesium ion. The most highly conserved regions of the alignment are involved in binding the magnesium ion.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A [auth B]Holo-[acyl-carrier-protein] synthase