7C1K | pdb_00007c1k

Crystal structure of the starter condensation domain of rhizomide synthetase RzmA mutant R148A

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	e7c1kA1	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	e7c1kA2	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	e7c1kB1	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	e7c1kB2	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)
C	Condensation_N	e7c1kC2	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)
C	Condensation_C_2	e7c1kC1	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)
D	Condensation_N	e7c1kD1	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)
D	Condensation_C_2	e7c1kD2	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 (utative)
A	3.30.559.30	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Nonribosomal peptide synthetase, condensation domain	CATH (utative)
B	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (utative)
B	3.30.559.30	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Nonribosomal peptide synthetase, condensation domain	CATH (utative)
C	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (utative)
C	3.30.559.30	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Nonribosomal peptide synthetase, condensation domain	CATH (utative)
D	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (utative)
D	3.30.559.30	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Nonribosomal peptide synthetase, condensation domain	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	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, C, D	Non-ribosomal peptide synthetase modules	2,3-dihydroxybenzoate-serine ligase activity acid-amino acid ligase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity vitamin binding amide binding modified amino acid binding binding phosphopantetheine binding small molecule binding	enterobactin biosynthetic process polyketide metabolic process catechol-containing compound metabolic process secondary metabolic process antibiotic biosynthetic process siderophore biosynthetic process antibiotic metabolic process secondary metabolite biosynthetic process siderophore metabolic process lactone biosynthetic process catechol-containing compound biosynthetic process catechol-containing siderophore biosynthetic process enterobactin metabolic process macrolide biosynthetic process enterobactin biosynthetic process polyketide metabolic process catechol-containing compound metabolic process secondary metabolic process antibiotic biosynthetic process siderophore biosynthetic process antibiotic metabolic process secondary metabolite biosynthetic process siderophore metabolic process lactone biosynthetic process catechol-containing compound biosynthetic process catechol-containing siderophore biosynthetic process enterobactin metabolic process macrolide biosynthetic process macrolide metabolic process biosynthetic process peptide biosynthetic process polyketide biosynthetic process lactone metabolic process phenol-containing compound metabolic process phenol-containing compound biosynthetic process metabolic process cellular process nonribosomal peptide biosynthetic process peptide metabolic process amino acid activation amino acid activation for nonribosomal peptide biosynthetic process amino acid metabolic process primary metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol protein-containing complex catalytic complex enterobactin synthetase complex intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR006162	Phosphopantetheine attachment site	PTM
A, B, C, D	IPR009081	Phosphopantetheine binding ACP domain	Domain
A, B, C, D	IPR020806	Polyketide synthase-like, phosphopantetheine-binding domain	Domain
A, B, C, D	IPR010071	Amino acid adenylation domain	Domain
A, B, C, D	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
A, B, C, D	IPR020845	AMP-binding, conserved site	Conserved Site
A, B, C, D	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR045851	AMP-binding enzyme, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR042099	ANL, N-terminal domain	Homologous Superfamily
A, B, C, D	IPR001242	Condensation domain	Domain
A, B, C, D	IPR036736	ACP-like superfamily	Homologous Superfamily
A, B, C, D	IPR025110	AMP-binding enzyme, C-terminal domain	Domain
A, B, C, D	IPR000873	AMP-dependent synthetase/ligase domain	Domain
A, B, C, D	IPR001031	Thioesterase	Domain
A, B, C, D	IPR020802	Thioesterase TesA-like	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.