ID   ACADM_MACFA             Reviewed;         421 AA.
AC   Q8HXY8;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 40.
DE   RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial;
DE            Short=MCAD;
DE            EC=1.3.99.3;
DE   Flags: Precursor;
GN   Name=ACADM; ORFNames=QtrA-12403;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Temporal cortex;
RA   Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological
RT   disease genes.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme is specific for acyl chain lengths of 4 to
CC       16 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA +
CC       reduced acceptor.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-
CC       oxidation.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases
CC       of different substrate specificities are present in mammalian
CC       tissues.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
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DR   EMBL; AB083301; BAC20580.1; -; mRNA.
DR   HSSP; P11310; 1EGD.
DR   SMR; Q8HXY8; 35-421.
DR   HOVERGEN; Q8HXY8; -.
DR   BRENDA; 1.3.99.3; 3438.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006092; Acyl-CoA_DH_N.
DR   InterPro; IPR006090; Acyl-CoA_Oxase/DH_1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_M.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR013764; AcylCoA_oxidase/DH_1/2_C.
DR   Gene3D; G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
DR   Gene3D; G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
DR   Gene3D; G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 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   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   2: Evidence at transcript level;
KW   FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW   Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT       1     25       Mitochondrion (By similarity).
FT   CHAIN        26    421       Medium-chain specific acyl-CoA
FT                                dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000000503.
FT   NP_BIND     158    167       FAD (By similarity).
FT   NP_BIND     191    193       FAD (By similarity).
FT   NP_BIND     306    308       FAD (By similarity).
FT   NP_BIND     316    317       FAD (By similarity).
FT   NP_BIND     374    378       FAD (By similarity).
FT   NP_BIND     403    405       FAD (By similarity).
FT   REGION      278    281       Substrate binding (By similarity).
FT   ACT_SITE    401    401       Proton acceptor (By similarity).
FT   BINDING     167    167       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     402    402       Substrate; via amide nitrogen (By
FT                                similarity).
SQ   SEQUENCE   421 AA;  46626 MW;  DDA2F825B5AF9CC0 CRC64;
     MAAAFGRCCR VLRSISRFHW RSQHTKADRQ REPGLGFSFE FTEQQKEFQA TARKFAREEI
     IPVAAEYDKT GEYPVPLIRR AWELGLMNPH IPQNCGGLGL GTFDACLISE ELAYGCTGVQ
     TAIEGNSLGQ MPIIIAGNEQ QKKKYLGRMT EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG
     DEYIINGQKM WITNGGKASW YFLLARSDPD PKAPANKAFT GFIVEADTPG IQIGRKELNM
     GQRCSDTRGI VFEDVKVLKE NVLIGDGAGF KIAMGAFDKT RPTVSSGAVG LAQRALDEAT
     KYALERKTFG KLLIEHQAIS FMLAEMAMKV ELARMSYQRA AWEVDSGRRN TYYASIAKAF
     AGDIANQLAT DAVQIFGGNG FNTEYPVEKL MRDAKIYQIY EGTSQIQRLI IAREHIGKYK
     S
//