ID   Q91WS8_MOUSE            Unreviewed;       421 AA.
AC   Q91WS8;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   02-SEP-2026, entry version 123.
DE   RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00019125};
DE            EC=1.3.8.7 {ECO:0000256|ARBA:ARBA00012033};
GN   Name=Acadm {ECO:0000313|EMBL:AAH13498.1, ECO:0000313|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 {ECO:0000313|EMBL:AAH13498.1};
RN   [1] {ECO:0000313|EMBL:AAH13498.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N {ECO:0000313|EMBL:AAH13498.1};
RC   TISSUE=Kidney {ECO:0000313|EMBL:AAH13498.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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).
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 (FAO), breaking down fatty acids into acetyl-
CC       CoA and allowing the production of energy from fats. The first step of
CC       FAO consists in the proR-proR stereospecific alpha, beta-
CC       dehydrogenation of fatty acyl-CoA thioesters using the electron
CC       transfer flavoprotein (ETF) as their physiologic electron acceptor,
CC       resulting in the formation of trans-2-enoyl-CoA ((2E)-enoyl-CoA). ETF
CC       is the electron acceptor that transfers electrons to the main
CC       mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF
CC       dehydrogenase). Among the different mitochondrial acyl-CoA
CC       dehydrogenases, medium-chain specific acyl-CoA dehydrogenase has
CC       preference for fatty acyl-CoAs with saturated 6 to 12 carbons long
CC       primary chains, making it but can also catalyze longer chains such as
CC       C14 and C16. {ECO:0000256|ARBA:ARBA00094413}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium-chain 2,3-saturated fatty acyl-CoA + oxidized
CC         [electron-transfer flavoprotein] + H(+) = a medium-chain (2E)-enoyl-
CC         CoA + 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:0000256|ARBA:ARBA00048063};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14478;
CC         Evidence={ECO:0000256|ARBA:ARBA00048063};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=decanoyl-CoA + oxidized [electron-transfer flavoprotein] +
CC         H(+) = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein];
CC         Xref=Rhea:RHEA:48176, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:61406, ChEBI:CHEBI:61430;
CC         Evidence={ECO:0000256|ARBA:ARBA00047546};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48177;
CC         Evidence={ECO:0000256|ARBA:ARBA00047546};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoyl-CoA + oxidized [electron-transfer flavoprotein] +
CC         H(+) = (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:0000256|ARBA:ARBA00047893};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47297;
CC         Evidence={ECO:0000256|ARBA:ARBA00047893};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexanoyl-CoA + oxidized [electron-transfer flavoprotein] +
CC         H(+) = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein];
CC         Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC         Evidence={ECO:0000256|ARBA:ARBA00049192};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC         Evidence={ECO:0000256|ARBA:ARBA00049192};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=octanoyl-CoA + oxidized [electron-transfer flavoprotein] +
CC         H(+) = (2E)-octenoyl-CoA + reduced [electron-transfer flavoprotein];
CC         Xref=Rhea:RHEA:48180, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57386, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:62242;
CC         Evidence={ECO:0000256|ARBA:ARBA00048877};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48181;
CC         Evidence={ECO:0000256|ARBA:ARBA00048877};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxidized [electron-transfer flavoprotein] + hexadecanoyl-CoA +
CC         H(+) = (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:0000256|ARBA:ARBA00047916};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43449;
CC         Evidence={ECO:0000256|ARBA:ARBA00047916};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pentanoyl-CoA + oxidized [electron-transfer flavoprotein] +
CC         H(+) = (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:0000256|ARBA:ARBA00048499};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43457;
CC         Evidence={ECO:0000256|ARBA:ARBA00048499};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tetradecanoyl-CoA + oxidized [electron-transfer flavoprotein]
CC         + H(+) = (2E)-tetradecenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:47316, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:61405;
CC         Evidence={ECO:0000256|ARBA:ARBA00049038};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47317;
CC         Evidence={ECO:0000256|ARBA:ARBA00049038};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR634180-3, ECO:0000256|RuleBase:RU362125};
CC   -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005198}.
CC   -!- SUBUNIT: Homotetramer. Interacts with the heterodimeric electron
CC       transfer flavoprotein ETF. {ECO:0000256|ARBA:ARBA00064103}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC013498; AAH13498.1; -; mRNA.
DR   AlphaFoldDB; Q91WS8; -.
DR   PeptideAtlas; Q91WS8; -.
DR   AGR; MGI:87867; -.
DR   MGI; MGI:87867; Acadm.
DR   UniPathway; UPA00660; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0070991; F:medium-chain fatty acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IEA:UniProtKB-ARBA.
DR   GO; GO:0051791; P:medium-chain fatty acid metabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:UniProtKB-ARBA.
DR   CDD; cd01157; MCAD; 1.
DR   FunFam; 1.10.540.10:FF:000010; Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; 1.
DR   FunFam; 1.20.140.10:FF:000011; Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; 1.
DR   FunFam; 2.40.110.10:FF:000007; Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; 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; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR006091; AcylCoA_DH/ox_M.
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.
PE   2: Evidence at transcript level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR634180-3};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          42..151
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          157..255
FT                   /note="Acyl-CoA dehydrogenase/oxidase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          267..414
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   ACT_SITE        401
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634180-1"
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:0000256|PIRSR:PIRSR634180-3"
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:0000256|PIRSR:PIRSR634180-3"
FT   BINDING         306..308
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:0000256|PIRSR:PIRSR634180-3"
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:0000256|PIRSR:PIRSR634180-3"
FT   BINDING         374..378
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:0000256|PIRSR:PIRSR634180-3"
FT   BINDING         403..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:0000256|PIRSR:PIRSR634180-3"
SQ   SEQUENCE   421 AA;  46437 MW;  31E01704E3E189BB 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 TYYASIAKAC
     AGDIANQLAT DAVQIFGGYG FNTEYPVEKL MRDAKIYQIY EGTAQIQRLI IAREHIEKYK
     N
//