ID   ACADM_BOVIN             Reviewed;         421 AA.
AC   Q3SZB4; A7LFV4;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 35.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li H., Xu S., Gao X., Ren H., Li J.;
RT   "Association of bovine ACADM SNP with economic traits.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; EU009460; ABS70460.1; -; mRNA.
DR   EMBL; BC102989; AAI02990.1; -; mRNA.
DR   IPI; IPI00704474; -.
DR   RefSeq; NP_001068703.1; -.
DR   UniGene; Bt.61205; -.
DR   SMR; Q3SZB4; 36-420.
DR   Ensembl; ENSBTAG00000024240; Bos taurus.
DR   GeneID; 505968; -.
DR   KEGG; bta:505968; -.
DR   HOVERGEN; Q3SZB4; -.
DR   OMA; Q3SZB4; EYPVPLI.
DR   BRENDA; 1.3.99.3; 251.
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_0000281995.
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;  46573 MW;  C43979D54E7A3A8D CRC64;
     MIALFRRSCG VLRSLSHFDW RSQHTKTALQ REPGSGFSFE FTEQQKEFQA TARKFAREEI
     IPLAAEYDKT GEYPVPLIKR AWELGLMNTH IPESCGGLGL GTFDSCLISE ELAYGCTGVQ
     TAIEANSLGQ MPVIIAGNDQ QQKKYLGRMT EEPLMCAYCV TEPVAGSDVA GIKTKAEKKG
     DEYIINGQKM WITNGGKANW YFLLARSDPD PKAPASKAFT GFIVEADTPG VQIGRKELNM
     GQRCSDTRGI VFEDVRVPKE NVLIGEGAGF KIAMGAFDKT RPPVAAAAVG LAQRALDEAT
     KYALERKTFG KLLIEHQGIS FLLAEMAMKV ELARLSYQRA AWEVDSGRRN TYYASIAKAY
     AGDIANQLAS DAVQIFGGNG FNTEYPVEKL MRDAKIYQIY EGTAQIQRLI IAREHIGRYK
     K
//