Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF01648e7r49A1 A: a+b three layersX: Bacillus chorismate mutase-likeH: 4'-phosphopantetheinyl transferase (From Topology)T: 4'-phosphopantetheinyl transferaseF: PF01648ECOD (1.6)
C [auth B]PF01648e7r49B1 A: a+b three layersX: Bacillus chorismate mutase-likeH: 4'-phosphopantetheinyl transferase (From Topology)T: 4'-phosphopantetheinyl transferaseF: PF01648ECOD (1.6)
E [auth C]PF01648e7r49C1 A: a+b three layersX: Bacillus chorismate mutase-likeH: 4'-phosphopantetheinyl transferase (From Topology)T: 4'-phosphopantetheinyl transferaseF: PF01648ECOD (1.6)
B [auth H]PF00550e7r49H1 A: alpha bundlesX: ACP-likeH: Acyl-carrier protein (ACP) (From Topology)T: Acyl-carrier protein (ACP)F: PF00550ECOD (1.6)
D [auth E]PF00550e7r49E1 A: alpha bundlesX: ACP-likeH: Acyl-carrier protein (ACP) (From Topology)T: Acyl-carrier protein (ACP)F: PF00550ECOD (1.6)
FPF00550e7r49F1 A: alpha bundlesX: ACP-likeH: Acyl-carrier protein (ACP) (From Topology)T: Acyl-carrier protein (ACP)F: PF00550ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A,
C [auth B],
E [auth C]
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
B [auth H],
D [auth E],
F
PF00550Phosphopantetheine attachment site (PP-binding)Phosphopantetheine attachment siteA 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes memb ...A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A,
C [auth B],
E [auth C]
Holo-[acyl-carrier-protein] synthase
B [auth H],
D [auth E],
F
D-alanyl carrier protein 1