Annotations: 5ZW8

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5zw8a2	All alpha proteins	Bromodomain-like	Acyl-CoA dehydrogenase C-terminal domain-like	automated matches	automated matches	(Prodigiosinella confusarubida ) [TaxId: 104623 ],	SCOPe (2.08)
A	d5zw8a1	Multi-domain proteins (alpha and beta)	Acyl-CoA dehydrogenase NM domain-like	Acyl-CoA dehydrogenase NM domain-like	automated matches	automated matches	(Prodigiosinella confusarubida ) [TaxId: 104623 ],	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	Acyl-CoA_dh_M	e5zw8A3	A: beta complex topology	X: Acyl-CoA dehydrogenase middle domain-like (From Topology)	H: Acyl-CoA dehydrogenase middle domain-like (From Topology)	T: Acyl-CoA dehydrogenase middle domain-like	F: Acyl-CoA_dh_M	ECOD (1.6)
A	Acyl-CoA_dh_N	e5zw8A2	A: alpha arrays	X: Acyl-CoA dehydrogenase N-terminal domain-like (From Topology)	H: Acyl-CoA dehydrogenase N-terminal domain-like (From Topology)	T: Acyl-CoA dehydrogenase N-terminal domain-like	F: Acyl-CoA_dh_N	ECOD (1.6)
A	Acyl-CoA_dh_1	e5zw8A1	A: alpha bundles	X: Bromodomain-like	H: Acyl-CoA dehydrogenase C-terminal domain-like (From Topology)	T: Acyl-CoA dehydrogenase C-terminal domain-like	F: Acyl-CoA_dh_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.110.10	Mainly Beta	Beta Barrel	Butyryl-CoA Dehydrogenase, subunit A	domain 2	CATH (4.3.0)
A	1.20.140.10	Mainly Alpha	Up-down Bundle	Butyryl-CoA Dehydrogenase, subunit A	domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02771	Acyl-CoA dehydrogenase, N-terminal domain (Acyl-CoA_dh_N)	Acyl-CoA dehydrogenase, N-terminal domain	The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.	Domain
A	PF02770	Acyl-CoA dehydrogenase, middle domain (Acyl-CoA_dh_M)	Acyl-CoA dehydrogenase, middle domain	Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.	Domain
A	PF00441	Acyl-CoA dehydrogenase, C-terminal domain (Acyl-CoA_dh_1)	Acyl-CoA dehydrogenase, C-terminal domain	C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.	Domain
A	PF08028	Acyl-CoA dehydrogenase, C-terminal domain (Acyl-CoA_dh_2)	Acyl-CoA dehydrogenase, C-terminal domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	L-prolyl-[peptidyl-carrier protein] dehydrogenase	oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor oxidoreductase activity acyl-CoA dehydrogenase activity oxidoreductase activity, acting on the CH-CH group of donors catalytic activity flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	antibiotic metabolic process biosynthetic process metabolic process cellular process antibiotic biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR009100	Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily	Homologous Superfamily
A	IPR046373	Acyl-CoA oxidase/dehydrogenase, middle domain superfamily	Homologous Superfamily
A	IPR006091	Acyl-CoA oxidase/dehydrogenase, middle domain	Domain
A	IPR009075	Acyl-CoA dehydrogenase/oxidase, C-terminal	Domain
A	IPR036250	Acyl-CoA dehydrogenase-like, C-terminal	Homologous Superfamily
A	IPR013786	Acyl-CoA dehydrogenase/oxidase, N-terminal	Domain
A	IPR037069	Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily	Homologous Superfamily

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.