Annotations: 5CZC

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	EUF08355	e5czcA1	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: EUF08355	ECOD (1.6)
A	Acyl_transf_1_1st	e5czcA2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: Acyl_transf_1_1st	ECOD (1.6)
B	EUF08355	e5czcB1	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: EUF08355	ECOD (1.6)
B	Acyl_transf_1_1st	e5czcB2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: Acyl_transf_1_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.366.10	Alpha Beta	3-Layer(aba) Sandwich	Malonyl-Coenzyme A Acyl Carrier Protein	domain 2	CATH (4.3.0)
B	3.40.366.10	Alpha Beta	3-Layer(aba) Sandwich	Malonyl-Coenzyme A Acyl Carrier Protein	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF21124	VinK acyltransferase small domain (VinK_C)	VinK acyltransferase small domain	This family includes the VinK acyltransferase. VinK transfers a dipeptide group between two ACPs, VinL and VinP1LdACP, in vicenistatin biosynthesis [1]. This entry represents the small C-terminal domain [1]. VinK has two conserved catalytic residues, ...	This family includes the VinK acyltransferase. VinK transfers a dipeptide group between two ACPs, VinL and VinP1LdACP, in vicenistatin biosynthesis [1]. This entry represents the small C-terminal domain [1]. VinK has two conserved catalytic residues, Ser-106 and His-216, at the interface between the large domain and small domain [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	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 cation binding ion binding binding metal ion binding small molecule binding	fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid 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 biosynthetic process small molecule metabolic process metabolic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid 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 biosynthetic 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
A, B	IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase	Homologous Superfamily
A, B	IPR001227	Acyl transferase domain superfamily	Homologous Superfamily
A, B	IPR050858	Malonyl CoA-ACP Transacylase/Polyketide Synthase FabD	Family
A, B	IPR049416	Malonyl-CoA-[acyl-carrier-protein] transacylase, small domain	Domain

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 R01GM157729.