Detail Information for IndEnz0002018536
IED ID IndEnz0002018536
Enzyme Type ID protease018536
Protein Name Acyl-CoA dehydrogenase family member 11
ACAD-11
EC 1.3.8.-
Gene Name Acad11
Organism Rattus norvegicus (Rat)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MEMDVTRDTVEVLPQHKFDIRSLEAYLNQHLPGFGSDHRAVLTVTQYRSGQSNPTFFLQKGSQAYVLRKKPPGSLLPKAHKIDREFKVQKALFSVGFPVPKPLLYCSNASIIGTEFYVMEHVQGRIFRDFSIPGVSPAERAAIYVSLVETLAWLHSLDIHSLGLDRYGTGVGYCKRQVSTWTKQYQASAHQSIPAMDQLSTWLMRNLPDSDNEECLVHGDFKLDNIVFHPKECRVIAVLDWELSTFGHPLSDLAHLSLFYFWPRTLPMINRGSHIQENTGIPLMEELISIYCRRRGIDPNLPNWNFFMALSFFKLAGIAQGVYSRYLMGNNSSEDSFLTANTVQPLAETGLQLSRRTLSTVPPQADAKSRLFAQSRRGQEVLTRVKQFMKQHVFPAEKEVAEYYAQNGNSAEKWEHPLVIEKLKEMAKAEGLWNLFLPAVSGLSQVDYALIAEETGKCFFAPDVFNCQAPDTGNMEVLHLYGSEQQKQQWLEPLLRGDITSVFCMTEPNVSSSDATNMECSIQRDGGSYIVHGKKWWSSGAGNPKCKIAVVLGRTESPSVSRHKVHSMILVPMDTPGVELIRPLSVFGYMDNVHGGHWEVHFNHVRVPASNLILGEGRGFEISQGRLGPGRIHHCMRSVGLAERILQIMCDRAVQREAFGKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAHSIDTLGSAAARKEIAMIKVAAPKAVCKIADRAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVHLSAIAKMELQDQARQLKARM
Enzyme Length 779
Uniprot Accession Number B3DMA2
Absorption
Active Site
Activity Regulation
Binding Site BINDING 513; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000250; BINDING 539; /note=FAD; /evidence=ECO:0000250; BINDING 656; /note=FAD; /evidence=ECO:0000250; BINDING 656; /note=FAD; shared with dimeric partner; /evidence=ECO:0000250; BINDING 726; /note=FAD; /evidence=ECO:0000250; BINDING 754; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250; BINDING 757; /note=FAD; /evidence=ECO:0000250
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:44704, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; Evidence={ECO:0000250|UniProtKB:Q709F0};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44705; Evidence={ECO:0000250|UniProtKB:Q709F0}; CATALYTIC ACTIVITY: Reaction=docosanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-docosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47228, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:65059, ChEBI:CHEBI:74692; Evidence={ECO:0000250|UniProtKB:Q709F0};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229; Evidence={ECO:0000250|UniProtKB:Q709F0}; CATALYTIC ACTIVITY: Reaction=H(+) + oxidized [electron-transfer flavoprotein] + tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47232, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693; Evidence={ECO:0000250|UniProtKB:Q709F0};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233; Evidence={ECO:0000250|UniProtKB:Q709F0}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:74691; Evidence={ECO:0000250|UniProtKB:Q709F0};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237; Evidence={ECO:0000250|UniProtKB:Q709F0}; CATALYTIC ACTIVITY: Reaction=H(+) + hexacosanoyl-CoA + oxidized [electron-transfer flavoprotein] = (2E)-hexacosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48216, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:64868, ChEBI:CHEBI:74281; Evidence={ECO:0000250|UniProtKB:Q709F0};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48217; Evidence={ECO:0000250|UniProtKB:Q709F0}; CATALYTIC ACTIVITY: Reaction=H(+) + oxidized [electron-transfer flavoprotein] + tricosanoyl-CoA = (2E)-tricosenoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:48220, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:90118, ChEBI:CHEBI:90119; Evidence={ECO:0000250|UniProtKB:Q709F0};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48221; Evidence={ECO:0000250|UniProtKB:Q709F0};
DNA Binding
EC Number 1.3.8.-
Enzyme Function FUNCTION: Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA. Probably participates in beta-oxydation and energy production but could also play a role in the metabolism of specific fatty acids to control fatty acids composition of cellular lipids in brain. {ECO:0000250|UniProtKB:Q709F0}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000250|UniProtKB:Q709F0}.
nucleotide Binding NP_BIND 503..513; /note=FAD; /evidence=ECO:0000250; NP_BIND 503..506; /note=FAD; /evidence=ECO:0000250; NP_BIND 511..513; /note=FAD; /evidence=ECO:0000250; NP_BIND 537..539; /note=FAD; /evidence=ECO:0000250; NP_BIND 726..730; /note=FAD; shared with dimeric partner; /evidence=ECO:0000250; NP_BIND 755..757; /note=FAD; /evidence=ECO:0000250
Features Binding site (7); Chain (1); Modified residue (6); Nucleotide binding (6); Region (1)
Keywords Acetylation;FAD;Fatty acid metabolism;Flavoprotein;Lipid metabolism;Membrane;Mitochondrion;Oxidoreductase;Peroxisome;Phosphoprotein;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:14561759}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q709F0}.
Modified Residue MOD_RES 175; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q80XL6; MOD_RES 210; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q80XL6; MOD_RES 323; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:Q80XL6; MOD_RES 368; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q80XL6; MOD_RES 390; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q80XL6; MOD_RES 765; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q80XL6
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 87,371
Kinetics
Metal Binding
Rhea ID RHEA:44704; RHEA:44705; RHEA:47228; RHEA:47229; RHEA:47232; RHEA:47233; RHEA:47236; RHEA:47237; RHEA:48216; RHEA:48217; RHEA:48220; RHEA:48221
Cross Reference Brenda