8CA1

Cryo-EM structure of the ACADVL dimer from Mus musculus.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000062	molecular_function	fatty-acyl-CoA binding
A	0001659	biological_process	temperature homeostasis
A	0003995	molecular_function	acyl-CoA dehydrogenase activity
A	0004466	molecular_function	long-chain fatty acyl-CoA dehydrogenase activity
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0009062	biological_process	fatty acid catabolic process
A	0009409	biological_process	response to cold
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0017099	molecular_function	very-long-chain fatty acyl-CoA dehydrogenase activity
A	0030855	biological_process	epithelial cell differentiation
A	0031966	cellular_component	mitochondrial membrane
A	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
A	0042645	cellular_component	mitochondrial nucleoid
A	0042802	molecular_function	identical protein binding
A	0045717	biological_process	negative regulation of fatty acid biosynthetic process
A	0046322	biological_process	negative regulation of fatty acid oxidation
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0090181	biological_process	regulation of cholesterol metabolic process
B	0000062	molecular_function	fatty-acyl-CoA binding
B	0001659	biological_process	temperature homeostasis
B	0003995	molecular_function	acyl-CoA dehydrogenase activity
B	0004466	molecular_function	long-chain fatty acyl-CoA dehydrogenase activity
B	0005654	cellular_component	nucleoplasm
B	0005730	cellular_component	nucleolus
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006635	biological_process	fatty acid beta-oxidation
B	0009062	biological_process	fatty acid catabolic process
B	0009409	biological_process	response to cold
B	0016491	molecular_function	oxidoreductase activity
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0017099	molecular_function	very-long-chain fatty acyl-CoA dehydrogenase activity
B	0030855	biological_process	epithelial cell differentiation
B	0031966	cellular_component	mitochondrial membrane
B	0033539	biological_process	fatty acid beta-oxidation using acyl-CoA dehydrogenase
B	0042645	cellular_component	mitochondrial nucleoid
B	0042802	molecular_function	identical protein binding
B	0045717	biological_process	negative regulation of fatty acid biosynthetic process
B	0046322	biological_process	negative regulation of fatty acid oxidation
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0090181	biological_process	regulation of cholesterol metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00072
Number of Residues	13
Details	ACYL_COA_DH_1 Acyl-CoA dehydrogenases signature 1. CLTEpsSGSDvaS

Chain	Residue	Details
B	CYS216-SER228

---

site_id	PS00073
Number of Residues	20
Details	ACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiMGGmGFmkEpgveRvlrD

Chain	Residue	Details
B	GLN436-ASP455

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	66
Details	Region: {"description":"Membrane-anchoring","evidences":[{"source":"UniProtKB","id":"P49748","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P49748","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P49748","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"23281369","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P49748","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---