5INI

Structural basis for acyl-CoA carboxylase-mediated assembly of unusual polyketide synthase extender units incorporated into the stambomycin antibiotics

External Resource: Annotation

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

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5inia1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Streptomyces ambofaciens ATCC 23877 ) [TaxId: 278992 ],	SCOPe (2.08)
F	d5inif1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Streptomyces ambofaciens ATCC 23877 ) [TaxId: 278992 ],	SCOPe (2.08)
B	d5inib1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Streptomyces ambofaciens ATCC 23877 ) [TaxId: 278992 ],	SCOPe (2.08)
C	d5inic1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Streptomyces ambofaciens ATCC 23877 ) [TaxId: 278992 ],	SCOPe (2.08)
D	d5inid1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Streptomyces ambofaciens ATCC 23877 ) [TaxId: 278992 ],	SCOPe (2.08)
E	d5inie1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Streptomyces ambofaciens ATCC 23877 ) [TaxId: 278992 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Carboxyl_trans_C	e5iniA2	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: Carboxyl_trans_C	ECOD (1.6)
F	Carboxyl_trans_C	e5iniF1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: Carboxyl_trans_C	ECOD (1.6)
B	Carboxyl_trans_C	e5iniB2	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: Carboxyl_trans_C	ECOD (1.6)
C	Carboxyl_trans_C	e5iniC1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: Carboxyl_trans_C	ECOD (1.6)
D	Carboxyl_trans_C	e5iniD1	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: Carboxyl_trans_C	ECOD (1.6)
E	Carboxyl_trans_C	e5iniE2	A: a/b three-layered sandwiches	X: ClpP/crotonase (From Topology)	H: ClpP/crotonase (From Topology)	T: ClpP/crotonase	F: Carboxyl_trans_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
F	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
B	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
C	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
D	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
E	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF01039	Carboxyl transferase domain (Carboxyl_trans)	Carboxyl transferase domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Putative carboxyl transferase	CoA carboxylase activity acetyl-CoA carboxylase activity ligase activity, forming carbon-carbon bonds catalytic activity ligase activity propionyl-CoA carboxylase activity transferase activity	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	acetyl-CoA carboxylase complex protein-containing complex cellular anatomical structure intracellular anatomical structure catalytic complex cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR011763	Acetyl-coenzyme A carboxyltransferase, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR029045	ClpP/crotonase-like domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR011762	Acetyl-coenzyme A carboxyltransferase, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F	IPR000438	Acetyl-CoA carboxylase carboxyl transferase, beta subunit	Family
A, B, C, D, E A, B, C, D, E, F	IPR034733	Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta	Domain
A, B, C, D, E A, B, C, D, E, F	IPR051047	Acyl-CoA Carboxylase Beta Subunit	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 R01GM157729.