4JN5

Crystal structures of the first condensation domain of the CDA synthetase

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Condensation_N	e4jn5A2	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: Condensation_N	ECOD (1.6)
A	Condensation_C_2	e4jn5A1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: Condensation_C_2	ECOD (1.6)
B	Condensation_N	e4jn5B2	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: Condensation_N	ECOD (1.6)
B	Condensation_C_2	e4jn5B1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: Condensation_C_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
A	3.30.559.30	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Nonribosomal peptide synthetase, condensation domain	CATH (4.3.0)
B	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
B	3.30.559.30	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Nonribosomal peptide synthetase, condensation domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00668	Condensation domain (Condensation)	Condensation domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	CDA peptide synthetase I	vitamin binding amide binding modified amino acid binding binding phosphopantetheine binding small molecule binding catalytic activity	biosynthetic process lipid biosynthetic process primary metabolic process metabolic process lipid metabolic process antibiotic metabolic process antibiotic biosynthetic process amino acid activation peptide biosynthetic process amino acid activation for nonribosomal peptide biosynthetic process amino acid metabolic process nonribosomal peptide biosynthetic process peptide metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR006162	Phosphopantetheine attachment site	PTM
A, B	IPR009081	Phosphopantetheine binding ACP domain	Domain
A, B	IPR010071	Amino acid adenylation domain	Domain
A, B	IPR020845	AMP-binding, conserved site	Conserved Site
A, B	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily	Homologous Superfamily
A, B	IPR010060	Non-ribosomal peptide synthase	Domain
A, B	IPR045851	AMP-binding enzyme, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR042099	ANL, N-terminal domain	Homologous Superfamily
A, B	IPR020806	Polyketide synthase, phosphopantetheine-binding domain	Domain
A, B	IPR001242	Condensation domain	Domain
A, B	IPR036736	ACP-like superfamily	Homologous Superfamily
A, B	IPR025110	AMP-binding enzyme, C-terminal domain	Domain
A, B	IPR000873	AMP-dependent synthetase/ligase 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.