6SMD

PlMCAT:AntF (holo): type II PKS acyl-carrier protein in complex with its malonyl-transacylase

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2 Family	Probable ACP-binding domain of malonyl-CoA ACP transacylase	8101067	4001289	SCOP2 (2022-06-29)
B	SCOP2 Family	FabD-like	8099999	4003614	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Probable ACP-binding domain of malonyl-CoA ACP transacylase	8101068	3001224	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	FabD/lysophospholipase-like	8100000	3001121	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	FabD/lysophospholipase-like	8100000	3001121	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Probable ACP-binding domain of malonyl-CoA ACP transacylase	8101068	3001224	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	FabD/lysophospholipase-like	8100000	3001121	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00550	e6smdA1	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PF00550	ECOD (1.6)
B	F_UNCLASSIFIED	e6smdB2	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF00698	e6smdB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)
C	F_UNCLASSIFIED	e6smdC1	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: F_UNCLASSIFIED	ECOD (1.6)
C	PF00698	e6smdC2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: PF00698	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.366.10	Alpha Beta	3-Layer(aba) Sandwich	Malonyl-Coenzyme A Acyl Carrier Protein	domain 2	CATH (utative)
B	3.30.70.250	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Malonyl-CoA ACP transacylase, ACP-binding	CATH (utative)
C	3.40.366.10	Alpha Beta	3-Layer(aba) Sandwich	Malonyl-Coenzyme A Acyl Carrier Protein	domain 2	CATH (utative)
C	3.30.70.250	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Malonyl-CoA ACP transacylase, ACP-binding	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00550	Phosphopantetheine attachment site (PP-binding)	Phosphopantetheine attachment site	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 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
B, C	PF00698	Acyl transferase domain (Acyl_transf_1)	Acyl transferase domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Acyl carrier protein	-	-	-
B, C	Malonyl CoA-acyl carrier protein transacylase	malonyltransferase activity acyltransferase activity [acyl-carrier-protein] S-malonyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity S-acyltransferase activity catalytic activity S-malonyltransferase activity	fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process biosynthetic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process biosynthetic process organic substance biosynthetic process cellular lipid metabolic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B, C	IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase	Homologous Superfamily
B, C	IPR024925	Malonyl CoA-acyl carrier protein transacylase	Family
B, C	IPR001227	Acyl transferase domain superfamily	Homologous Superfamily
B, C	IPR016036	Malonyl-CoA ACP transacylase, ACP-binding	Homologous Superfamily
B, C	IPR014043	Acyl transferase	Domain
B, C	IPR004410	Malonyl CoA-acyl carrier protein transacylase, FabD-type	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.