ACADL_RAT
ID ACADL_RAT Reviewed; 430 AA.
AC P15650;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Long-chain specific acyl-CoA dehydrogenase, mitochondrial;
DE Short=LCAD;
DE EC=1.3.8.8 {ECO:0000269|PubMed:15466478, ECO:0000269|PubMed:3968063};
DE Flags: Precursor;
GN Name=Acadl {ECO:0000312|RGD:2011};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2777793; DOI=10.1016/s0021-9258(18)71624-4;
RA Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J.,
RA Ikeda Y., Kraus J., Tanaka K.;
RT "Molecular cloning and nucleotide sequence of cDNAs encoding the precursors
RT of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and
RT isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of
RT the acyl-CoA dehydrogenase family.";
RL J. Biol. Chem. 264:16321-16331(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Aorta;
RX PubMed=8268228; DOI=10.1016/0167-4781(93)90015-6;
RA Hainline B.E., Kahlenbeck D.J., Grant J., Strauss A.W.;
RT "Tissue specific and developmental expression of rat long- and medium-chain
RT acyl-CoA dehydrogenases.";
RL Biochim. Biophys. Acta 1216:460-468(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 52-61 AND 255-267, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=3968063; DOI=10.1016/s0021-9258(20)71245-7;
RA Ikeda Y., Okamura-Ikeda K., Tanaka K.;
RT "Purification and characterization of short-chain, medium-chain, and long-
RT chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the
RT holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme.";
RL J. Biol. Chem. 260:1311-1325(1985).
RN [6]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=3813556; DOI=10.1016/0003-9861(87)90072-5;
RA Ikeda Y., Keese S.M., Fenton W.A., Tanaka K.;
RT "Biosynthesis of four rat liver mitochondrial acyl-CoA dehydrogenases: in
RT vitro synthesis, import into mitochondria, and processing of their
RT precursors in a cell-free system and in cultured cells.";
RL Arch. Biochem. Biophys. 252:662-674(1987).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15466478; DOI=10.1074/jbc.m409640200;
RA Yu W., Liang X., Ensenauer R.E., Vockley J., Sweetman L., Schulz H.;
RT "Leaky beta-oxidation of a trans-fatty acid: incomplete beta-oxidation of
RT elaidic acid is due to the accumulation of 5-trans-tetradecenoyl-CoA and
RT its hydrolysis and conversion to 5-trans-tetradecenoylcarnitine in the
RT matrix of rat mitochondria.";
RL J. Biol. Chem. 279:52160-52167(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-55, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Long-chain specific acyl-CoA dehydrogenase is one of the
CC acyl-CoA dehydrogenases that catalyze the first step of mitochondrial
CC fatty acid beta-oxidation, an aerobic process breaking down fatty acids
CC into acetyl-CoA and allowing the production of energy from fats
CC (PubMed:3968063). The first step of fatty acid beta-oxidation consists
CC in the removal of one hydrogen from C-2 and C-3 of the straight-chain
CC fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-
CC CoA (PubMed:3968063). Among the different mitochondrial acyl-CoA
CC dehydrogenases, long-chain specific acyl-CoA dehydrogenase can act on
CC saturated and unsaturated acyl-CoAs with 6 to 24 carbons with a
CC preference for 8 to 18 carbons long primary chains (PubMed:3968063,
CC PubMed:15466478). {ECO:0000269|PubMed:15466478,
CC ECO:0000269|PubMed:3968063, ECO:0000303|PubMed:3968063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA +
CC reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721,
CC Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83721,
CC ChEBI:CHEBI:83727; EC=1.3.8.8; Evidence={ECO:0000269|PubMed:15466478,
CC ECO:0000269|PubMed:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17722;
CC Evidence={ECO:0000305|PubMed:3968063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + octanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-octenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48180, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:62242;
CC Evidence={ECO:0000269|PubMed:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48181;
CC Evidence={ECO:0000305|PubMed:3968063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-decenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48176, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:61406, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000269|PubMed:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177;
CC Evidence={ECO:0000305|PubMed:3968063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-dodecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47296, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC Evidence={ECO:0000269|PubMed:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297;
CC Evidence={ECO:0000305|PubMed:3968063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC tetradecanoyl-CoA = (2E)-tetradecenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:61405;
CC Evidence={ECO:0000269|PubMed:15466478, ECO:0000269|PubMed:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317;
CC Evidence={ECO:0000305|PubMed:3968063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexadecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43448, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:61526;
CC Evidence={ECO:0000269|PubMed:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449;
CC Evidence={ECO:0000305|PubMed:3968063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + octadecanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-octadecenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47240, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57394, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:71412;
CC Evidence={ECO:0000269|PubMed:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47241;
CC Evidence={ECO:0000305|PubMed:3968063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5E)-tetradecenoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E,5E)-tetradecadienoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:49828, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:131943, ChEBI:CHEBI:131944;
CC Evidence={ECO:0000269|PubMed:15466478};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49829;
CC Evidence={ECO:0000305|PubMed:3968063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z)-tetradecenoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E,5Z)-tetradecadienoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47448, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:84650, ChEBI:CHEBI:87701;
CC Evidence={ECO:0000269|PubMed:15466478};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47449;
CC Evidence={ECO:0000305|PubMed:3968063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E,9Z)-octadecadienoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47300, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:77553;
CC Evidence={ECO:0000269|PubMed:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47301;
CC Evidence={ECO:0000305|PubMed:3968063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000250|UniProtKB:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC Evidence={ECO:0000250|UniProtKB:P28330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:74691;
CC Evidence={ECO:0000250|UniProtKB:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237;
CC Evidence={ECO:0000250|UniProtKB:P28330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-docosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47228, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:65059, ChEBI:CHEBI:74692;
CC Evidence={ECO:0000250|UniProtKB:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229;
CC Evidence={ECO:0000250|UniProtKB:P28330};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47232, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693;
CC Evidence={ECO:0000250|UniProtKB:P28330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233;
CC Evidence={ECO:0000250|UniProtKB:P28330};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:3968063};
CC -!- ACTIVITY REGULATION: Inhibited by crotonyl-CoA, 2-octenoyl-CoA and 2-
CC hexadecenoyl-CoA. {ECO:0000269|PubMed:3968063}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=123 uM for octanoyl-CoA (at 32 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:3968063};
CC KM=24.3 uM for decanoyl-CoA (at 32 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:3968063};
CC KM=9 uM for dodecanoyl-CoA (at 32 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:3968063};
CC KM=7.4 uM for tetradecanoyl-CoA (at 32 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:3968063};
CC KM=2.5 uM for hexadecanoyl-CoA (at 32 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:3968063};
CC KM=5.4 uM for octadecanoyl-CoA (at 32 degrees Celsius and pH 8.0)
CC {ECO:0000269|PubMed:3968063};
CC KM=6.5 uM for (9Z)-octadecenoyl-CoA (at 32 degrees Celsius and pH
CC 8.0) {ECO:0000269|PubMed:3968063};
CC KM=0.41 uM for tetradecanoyl-CoA {ECO:0000269|PubMed:15466478};
CC KM=0.4 uM for (5Z)-tetradecenoyl-CoA {ECO:0000269|PubMed:15466478};
CC KM=1.6 uM for (5E)-tetradecenoyl-CoA {ECO:0000269|PubMed:15466478};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:3968063};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000303|PubMed:3968063}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:3813556,
CC ECO:0000269|PubMed:3968063}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:3813556}.
CC -!- PTM: Acetylation at Lys-318 and Lys-322 in proximity of the cofactor-
CC binding sites strongly reduces catalytic activity. These sites are
CC deacetylated by SIRT3. {ECO:0000250|UniProtKB:P51174}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; J05029; AAA40668.1; -; mRNA.
DR EMBL; L11276; AAA41514.1; -; mRNA.
DR EMBL; BC062006; AAH62006.1; -; mRNA.
DR PIR; A34252; A34252.
DR RefSeq; NP_036951.1; NM_012819.1.
DR AlphaFoldDB; P15650; -.
DR SMR; P15650; -.
DR BioGRID; 247326; 1.
DR IntAct; P15650; 11.
DR STRING; 10116.ENSRNOP00000017686; -.
DR ChEMBL; CHEMBL2176836; -.
DR SwissLipids; SLP:000001586; -.
DR CarbonylDB; P15650; -.
DR iPTMnet; P15650; -.
DR PhosphoSitePlus; P15650; -.
DR jPOST; P15650; -.
DR PaxDb; P15650; -.
DR PRIDE; P15650; -.
DR Ensembl; ENSRNOT00000017686; ENSRNOP00000017686; ENSRNOG00000012966.
DR GeneID; 25287; -.
DR KEGG; rno:25287; -.
DR UCSC; RGD:2011; rat.
DR CTD; 33; -.
DR RGD; 2011; Acadl.
DR eggNOG; KOG0141; Eukaryota.
DR GeneTree; ENSGT00940000157652; -.
DR HOGENOM; CLU_018204_0_3_1; -.
DR InParanoid; P15650; -.
DR OMA; QWEKDGI; -.
DR OrthoDB; 589058at2759; -.
DR PhylomeDB; P15650; -.
DR TreeFam; TF105054; -.
DR Reactome; R-RNO-77285; Beta oxidation of myristoyl-CoA to lauroyl-CoA.
DR Reactome; R-RNO-77310; Beta oxidation of lauroyl-CoA to decanoyl-CoA-CoA.
DR SABIO-RK; P15650; -.
DR UniPathway; UPA00660; -.
DR PRO; PR:P15650; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000012966; Expressed in heart and 19 other tissues.
DR Genevisible; P15650; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:BHF-UCL.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:RGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IDA:RGD.
DR GO; GO:0016401; F:palmitoyl-CoA oxidase activity; ISO:RGD.
DR GO; GO:0042413; P:carnitine catabolic process; ISO:RGD.
DR GO; GO:0019254; P:carnitine metabolic process, CoA-linked; ISO:RGD.
DR GO; GO:0044242; P:cellular lipid catabolic process; ISO:RGD.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:RGD.
DR GO; GO:0009062; P:fatty acid catabolic process; ISO:RGD.
DR GO; GO:0042758; P:long-chain fatty acid catabolic process; IDA:RGD.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; ISO:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:RGD.
DR GO; GO:0009409; P:response to cold; ISO:RGD.
DR GO; GO:0001659; P:temperature homeostasis; ISO:RGD.
DR CDD; cd01160; LCAD; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR034179; LCAD.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; FAD; Fatty acid metabolism;
KW Flavoprotein; Lipid metabolism; Mitochondrion; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2777793"
FT CHAIN 31..430
FT /note="Long-chain specific acyl-CoA dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000000513"
FT ACT_SITE 291
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 170..179
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 203..205
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 227..228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 289..292
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 328
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 385..389
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 412..413
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT BINDING 414..416
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P26440"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 66
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 66
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 81
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 81
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 165
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 240
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 254
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 254
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 279
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 279
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 322
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 322
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 358
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51174"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51174"
SQ SEQUENCE 430 AA; 47873 MW; BEE1C7E0FDD84D2E CRC64;
MAARLLLRSL RVLSARSATL PPPSARCSHS GAEARLETPS AKKLTDIGIR RIFSSEHDIF
RESVRKFFQE EVIPYHEEWE KAGEVSRELW EKAGKQGLLG INIAEKHGGI GGDLLSTAVT
WEEQAYSNCT GPGFSLHSDI VMPYIANYGT KEQIEQFIPQ MTAGKCIGAI AMTEPGAGSD
LQGVRTNAKR SGSDWILNGS KVFITNGWLS DLVIVVAVTN REARSPAHGI SLFLVENGMK
GFIKGKKLHK MGMKAQDTAE LFFEDVRLPA SALLGEENKG FYYLMQELPQ ERLLIADLAI
SACEFMFEET RNYVRQRKAF GKTVAHIQTV QHKLAELKTN ICVTRAFVDS CLQLHETKRL
DSASASMAKY WASELQNTVA YQCVQLHGGW GYMWEYPIAK AYVDARVQPI YGGTNEIMKE
LIARQIVSDS
