ID   ACADM_CAEEL             Reviewed;         417 AA.
AC   Q22347;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 74.
DE   RecName: Full=Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial;
DE            Short=MCAD;
DE            EC=1.3.99.3;
DE   Flags: Precursor;
GN   ORFNames=T08G2.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
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   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
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DR   EMBL; U42838; AAB52493.1; -; Genomic_DNA.
DR   PIR; T16838; T16838.
DR   RefSeq; NP_510788.1; -.
DR   UniGene; Cel.378; -.
DR   HSSP; P11310; 1EGE.
DR   DIP; DIP:25385N; -.
DR   IntAct; Q22347; 2.
DR   Ensembl; T08G2.3; Caenorhabditis elegans.
DR   GeneID; 181757; -.
DR   KEGG; cel:T08G2.3; -.
DR   WormBase; WBGene00020366; T08G2.3.
DR   WormPep; T08G2.3; CE07473.
DR   OMA; Q22347; SACCITE.
DR   BRENDA; 1.3.99.3; 672.
DR   NextBio; 915218; -.
DR   ArrayExpress; Q22347; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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   Complete proteome; FAD; Fatty acid metabolism; Flavoprotein;
KW   Lipid metabolism; Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT       1     15       Mitochondrion (By similarity).
FT   CHAIN        16    417       Probable medium-chain specific acyl-CoA
FT                                dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000000507.
FT   NP_BIND     148    157       FAD (By similarity).
FT   NP_BIND     181    183       FAD (By similarity).
FT   NP_BIND     306    307       FAD (By similarity).
FT   NP_BIND     364    368       FAD (By similarity).
FT   NP_BIND     393    395       FAD (By similarity).
FT   REGION      268    271       Substrate binding (By similarity).
FT   ACT_SITE    391    391       Proton acceptor (By similarity).
FT   BINDING     157    157       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     392    392       Substrate; via amide nitrogen (By
FT                                similarity).
SQ   SEQUENCE   417 AA;  44818 MW;  98CE260E72C521BF CRC64;
     MLSRIATSSL GLSRSATGVI ATQSRQISFD LSETQKEIQD AALKFSKDVL VPNAAKFDES
     GEFPWEIVRQ AHSLGLMNPQ IPEKYGGPGM TTLETALIVE ALSYGCTGIQ LGIMGPSLAI
     APVYISGNEE QKKKYLGALA AEPIIASYCV TEPGAGSDVN GVKTKCEKKG DEYIINGSKA
     WITGGGHAKW FFVLARSDPN PKTPAGKAFT AFIVDGDTPG ITRGKKEKNM GQRCSDTRVI
     TFEDVRVPAE NVLGAPGAGF KVAMEAFDMT RPGVAAGALG LSWRCLDESA KYALERKAFG
     TVIANHQAVQ FMLADMAVNL ELARLITYKS ANDVDNKVRS SYNASIAKCF AADTANQAAT
     NAVQIFGGNG FNSEYPVEKL MRDAKIYQIY EGTSQIQRIV ISRMLLGHFA QNGTSRI
//