ID   ACADM_MOUSE             Reviewed;         421 AA.
AC   P45952; Q64235;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000305|PubMed:7829081};
DE            Short=MCAD {ECO:0000303|PubMed:7829081};
DE            EC=1.3.8.7 {ECO:0000269|PubMed:16121256};
DE   Flags: Precursor;
GN   Name=Acadm {ECO:0000312|MGI:MGI:87867};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RX   PubMed=7829081; DOI=10.1006/geno.1994.1486;
RA   Tolwani R.J., Farmer S.C., Wood P.A.;
RT   "Molecular cloning and characterization of the mouse medium-chain acyl-CoA
RT   dehydrogenase cDNA.";
RL   Genomics 23:247-249(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-193.
RX   PubMed=1438358;
RA   Wood P.A., Farmer S.C., Tolwani R.J., Warren J.R., Steinkampf M.P.,
RA   Johnson L.W., Mountz J.D., Kelly D.P.;
RT   "Molecular studies of mouse medium and long-chain acyl-CoA dehydrogenase
RT   genes for site-directed mutagenesis of embryonic stem cells.";
RL   Prog. Clin. Biol. Res. 375:151-160(1992).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX   PubMed=16121256; DOI=10.1371/journal.pgen.0010023;
RA   Tolwani R.J., Hamm D.A., Tian L., Sharer J.D., Vockley J., Rinaldo P.,
RA   Matern D., Schoeb T.R., Wood P.A.;
RT   "Medium-chain acyl-CoA dehydrogenase deficiency in gene-targeted mice.";
RL   PLoS Genet. 1:e23-e23(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-351, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-69; LYS-179; LYS-212;
RP   LYS-217; LYS-235; LYS-259 AND LYS-271, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-69; LYS-79; LYS-212;
RP   LYS-217; LYS-235; LYS-259; LYS-271 AND LYS-301, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Medium-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:16121256). 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:16121256). Electron transfer flavoprotein (ETF) is the
CC       electron acceptor that transfers electrons to the main mitochondrial
CC       respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase)
CC       (By similarity). Among the different mitochondrial acyl-CoA
CC       dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts
CC       specifically on acyl-CoAs with saturated 6 to 12 carbons long primary
CC       chains (PubMed:16121256). {ECO:0000250|UniProtKB:P11310,
CC       ECO:0000269|PubMed:16121256}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC         [electron-transfer flavoprotein] = a medium-chain (2E)-enoyl-CoA +
CC         reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:14477,
CC         Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:83723,
CC         ChEBI:CHEBI:83726; EC=1.3.8.7;
CC         Evidence={ECO:0000269|PubMed:16121256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14478;
CC         Evidence={ECO:0000269|PubMed:16121256};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxidized [electron-transfer flavoprotein] + pentanoyl-
CC         CoA = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein];
CC         Xref=Rhea:RHEA:43456, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57389, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:86160;
CC         Evidence={ECO:0000250|UniProtKB:P08503};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43457;
CC         Evidence={ECO:0000250|UniProtKB:P08503};
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:P11310};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC         Evidence={ECO:0000250|UniProtKB:P11310};
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:16121256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48181;
CC         Evidence={ECO:0000269|PubMed:16121256};
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:0000250|UniProtKB:P11310};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177;
CC         Evidence={ECO:0000250|UniProtKB:P11310};
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:0000250|UniProtKB:P11310};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297;
CC         Evidence={ECO:0000250|UniProtKB:P11310};
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:0000250|UniProtKB:P11310};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317;
CC         Evidence={ECO:0000250|UniProtKB:P11310};
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:16121256};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449;
CC         Evidence={ECO:0000269|PubMed:16121256};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P11310};
CC   -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC       {ECO:0000269|PubMed:16121256}.
CC   -!- SUBUNIT: Homotetramer. Interacts with the heterodimeric electron
CC       transfer flavoprotein ETF. {ECO:0000250|UniProtKB:P11310}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P08503}.
CC   -!- PTM: Acetylated. Could occur at proximity of the cofactor-binding sites
CC       and reduce the catalytic activity. Could be deacetylated by SIRT3.
CC       {ECO:0000250|UniProtKB:P11310}.
CC   -!- DISRUPTION PHENOTYPE: Mice lacking Mcad show increased neonatal
CC       mortality (PubMed:16121256). They display hypothermia and cold
CC       intolerance upon fasting (PubMed:16121256). Their serum and bile
CC       acylcarnitine profile is also different from wild-type mice, with an
CC       elevation of serum decenoylcarnitine compared to wild-type mice
CC       (PubMed:16121256). They also display hepatic steatosis following fast
CC       periods (PubMed:16121256). They develop significantly elevated
CC       concentrations of urinary adipic, suberic, and sebacic acids and
CC       hexanoylglycine (PubMed:16121256). {ECO:0000269|PubMed:16121256}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U07159; AAA76733.1; -; mRNA.
DR   EMBL; S48761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S48759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS17924.1; -.
DR   PIR; A55724; A55724.
DR   RefSeq; NP_031408.1; NM_007382.5.
DR   AlphaFoldDB; P45952; -.
DR   SMR; P45952; -.
DR   BioGRID; 197912; 24.
DR   IntAct; P45952; 7.
DR   MINT; P45952; -.
DR   STRING; 10090.ENSMUSP00000072483; -.
DR   GlyGen; P45952; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P45952; -.
DR   PhosphoSitePlus; P45952; -.
DR   SwissPalm; P45952; -.
DR   EPD; P45952; -.
DR   jPOST; P45952; -.
DR   MaxQB; P45952; -.
DR   PaxDb; 10090-ENSMUSP00000072483; -.
DR   PeptideAtlas; P45952; -.
DR   ProteomicsDB; 296438; -.
DR   Pumba; P45952; -.
DR   Antibodypedia; 1642; 521 antibodies from 38 providers.
DR   DNASU; 11364; -.
DR   Ensembl; ENSMUST00000072697.13; ENSMUSP00000072483.7; ENSMUSG00000062908.13.
DR   GeneID; 11364; -.
DR   KEGG; mmu:11364; -.
DR   UCSC; uc008ruj.2; mouse.
DR   AGR; MGI:87867; -.
DR   CTD; 34; -.
DR   MGI; MGI:87867; Acadm.
DR   VEuPathDB; HostDB:ENSMUSG00000062908; -.
DR   eggNOG; KOG0140; Eukaryota.
DR   GeneTree; ENSGT00940000158429; -.
DR   HOGENOM; CLU_018204_0_2_1; -.
DR   InParanoid; P45952; -.
DR   OMA; KCHAADV; -.
DR   OrthoDB; 275353at2759; -.
DR   PhylomeDB; P45952; -.
DR   TreeFam; TF105020; -.
DR   Reactome; R-MMU-77288; mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
DR   Reactome; R-MMU-77346; Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
DR   Reactome; R-MMU-77348; Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
DR   UniPathway; UPA00660; -.
DR   BioGRID-ORCS; 11364; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Acadm; mouse.
DR   PRO; PR:P45952; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P45952; Protein.
DR   Bgee; ENSMUSG00000062908; Expressed in heart right ventricle and 267 other cell types or tissues.
DR   ExpressionAtlas; P45952; baseline and differential.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; ISO:MGI.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0016853; F:isomerase activity; ISO:MGI.
DR   GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IMP:BHF-UCL.
DR   GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR   GO; GO:0045329; P:carnitine biosynthetic process; ISO:MGI.
DR   GO; GO:0009437; P:carnitine metabolic process; IMP:MGI.
DR   GO; GO:0019254; P:carnitine metabolic process, CoA-linked; IMP:BHF-UCL.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:BHF-UCL.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0051793; P:medium-chain fatty acid catabolic process; ISO:MGI.
DR   GO; GO:0051791; P:medium-chain fatty acid metabolic process; IMP:BHF-UCL.
DR   GO; GO:0006082; P:organic acid metabolic process; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0006111; P:regulation of gluconeogenesis; IMP:BHF-UCL.
DR   GO; GO:0009409; P:response to cold; IMP:MGI.
DR   GO; GO:0042594; P:response to starvation; IMP:MGI.
DR   CDD; cd01157; MCAD; 1.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 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_sf.
DR   InterPro; IPR034180; MCAD.
DR   PANTHER; PTHR48083:SF2; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
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   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
DR   SWISS-2DPAGE; P45952; -.
DR   Genevisible; P45952; MM.
PE   1: Evidence at protein level;
KW   Acetylation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW   Mitochondrion; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P08503"
FT   CHAIN           26..421
FT                   /note="Medium-chain specific acyl-CoA dehydrogenase,
FT                   mitochondrial"
FT                   /id="PRO_0000000504"
FT   ACT_SITE        401
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         158..167
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         167
FT                   /ligand="octanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57386"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         191..193
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         216
FT                   /ligand="octanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57386"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         278
FT                   /ligand="octanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57386"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         281
FT                   /ligand="octanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57386"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         306..308
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         316..317
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         349
FT                   /ligand="octanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57386"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         351
FT                   /ligand="octanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57386"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         374..378
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         401
FT                   /ligand="octanoyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57386"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   BINDING         402..405
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P41367"
FT   MOD_RES         30
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         30
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         69
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         69
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         79
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         179
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         212
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         212
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         217
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         217
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         235
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         235
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         259
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         259
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         271
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         271
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         301
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         351
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        135
FT                   /note="L -> I (in Ref. 2; S48759)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="V -> A (in Ref. 2; S48761)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   421 AA;  46481 MW;  36976704E3E48CBB CRC64;
     MAAAFRRGCR VLRSVSHFEC RTQHSKAAHK QEPGLGFSFE LTEQQKEFQA TARKFAREEI
     IPVAPEYDKS GEYPFPLIKR AWELGLINAH IPESCGGLGL GTFDACLITE ELAYGCTGVQ
     TAIEANSLGQ MPVILAGNDQ QKKKYLGRMT EQPMMCAYCV TEPSAGSDVA AIKTKAEKKG
     DEYVINGQKM WITNGGKANW YFLLARSNPD PKVPASKAFT GFIVEADTPG IHIGKKELNM
     GQRCSDTRGI AFEDVRVPKE NVLIGEGAGF KIAMGAFDRT RPTVAAGAVG LAQRALDEAT
     KYALDRKTFG KLLVEHQGVS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN TYYASIAKAF
     AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY EGTAQIQRLI IAREHIEKYK
     N
//