3MFM

Crystal Structures and Mutational Analyses of Acyl-CoA Carboxylase Subunit of Streptomyces coelicolor

External Resource: Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth C]	d3mfmc1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Streptomyces coelicolor ) [TaxId: 1902 ],	SCOPe (2.08)
B [auth F]	d3mfmf1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Streptomyces coelicolor ) [TaxId: 1902 ],	SCOPe (2.08)
C [auth A]	d3mfma1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Streptomyces coelicolor ) [TaxId: 1902 ],	SCOPe (2.08)
D [auth B]	d3mfmb1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Streptomyces coelicolor ) [TaxId: 1902 ],	SCOPe (2.08)
E [auth D]	d3mfmd1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Streptomyces coelicolor ) [TaxId: 1902 ],	SCOPe (2.08)
F [auth E]	d3mfme1	Alpha and beta proteins (a/b)	ClpP/crotonase	ClpP/crotonase	automated matches	automated matches	(Streptomyces coelicolor ) [TaxId: 1902 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth C]	SCOP2B Superfamily	ClpP/crotonase	8044079	3000033	SCOP2B (2022-06-29)
A [auth C]	SCOP2B Superfamily	ClpP/crotonase	8044078	3000033	SCOP2B (2022-06-29)
B [auth F]	SCOP2B Superfamily	ClpP/crotonase	8044079	3000033	SCOP2B (2022-06-29)
B [auth F]	SCOP2B Superfamily	ClpP/crotonase	8044078	3000033	SCOP2B (2022-06-29)
C [auth A]	SCOP2B Superfamily	ClpP/crotonase	8044079	3000033	SCOP2B (2022-06-29)
C [auth A]	SCOP2B Superfamily	ClpP/crotonase	8044078	3000033	SCOP2B (2022-06-29)
D [auth B]	SCOP2B Superfamily	ClpP/crotonase	8044078	3000033	SCOP2B (2022-06-29)
D [auth B]	SCOP2B Superfamily	ClpP/crotonase	8044079	3000033	SCOP2B (2022-06-29)
E [auth D]	SCOP2B Superfamily	ClpP/crotonase	8044079	3000033	SCOP2B (2022-06-29)
E [auth D]	SCOP2B Superfamily	ClpP/crotonase	8044078	3000033	SCOP2B (2022-06-29)
F [auth E]	SCOP2B Superfamily	ClpP/crotonase	8044078	3000033	SCOP2B (2022-06-29)
F [auth E]	SCOP2B Superfamily	ClpP/crotonase	8044079	3000033	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 [auth C]	Carboxyl_trans_C	e3mfmC6	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 [auth F]	Carboxyl_trans_C	e3mfmF6	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 [auth A]	Carboxyl_trans_C	e3mfmA6	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 [auth B]	Carboxyl_trans_C	e3mfmB6	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 [auth D]	Carboxyl_trans_C	e3mfmD6	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 [auth E]	Carboxyl_trans_C	e3mfmE6	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 [auth C]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
B [auth F]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
C [auth A]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
D [auth B]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
E [auth D]	3.90.226.10	Alpha Beta	Alpha-Beta Complex	2-enoyl-CoA Hydratase	Chain A, domain 1	CATH (4.3.0)
F [auth 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 [auth C], B [auth F], C [auth A], D [auth B], E [auth D], A [auth C], B [auth F], C [auth A], D [auth B], E [auth D], F [auth E]	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 [auth C], B [auth F], C [auth A], D [auth B], E [auth D], A [auth C], B [auth F], C [auth A], D [auth B], E [auth D], F [auth E]	Propionyl-CoA carboxylase complex B subunit	CoA carboxylase activity acetyl-CoA carboxylase activity ligase activity, forming carbon-carbon bonds catalytic activity ligase 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 biosynthetic process cellular lipid metabolic 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 biosynthetic process cellular lipid metabolic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process	acetyl-CoA carboxylase complex protein-containing complex intracellular anatomical structure catalytic complex cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

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