| 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 |