ID   GCDH_MACFA              Reviewed;         438 AA.
AC   Q8HXX8;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 41.
DE   RecName: Full=Glutaryl-CoA dehydrogenase, mitochondrial;
DE            Short=GCD;
DE            EC=1.3.99.7;
DE   Flags: Precursor;
GN   Name=GCDH; ORFNames=QccE-20069;
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=Brain 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: Catalyzes the oxidative decarboxylation of glutaryl-CoA
CC       to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine,
CC       L-hydroxylysine, and L-tryptophan metabolism. It uses electron
CC       transfer flavoprotein as its electron acceptor (By similarity).
CC   -!- CATALYTIC ACTIVITY: Glutaryl-CoA + acceptor = crotonoyl-CoA +
CC       CO(2) + reduced acceptor.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Amino-acid metabolism; lysine degradation.
CC   -!- PATHWAY: Amino-acid metabolism; tryptophan metabolism.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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; AB083311; BAC20590.1; -; mRNA.
DR   HSSP; P15651; 1JQI.
DR   SMR; Q8HXX8; 47-436.
DR   HOVERGEN; Q8HXX8; -.
DR   BRENDA; 1.3.99.7; 3438.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004361; F:glutaryl-CoA dehydrogenase activity; IEA:EC.
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; Flavoprotein; Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT       1     44       Mitochondrion (Potential).
FT   CHAIN        45    438       Glutaryl-CoA dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000000527.
FT   NP_BIND     177    180       FAD (By similarity).
FT   NP_BIND     212    214       FAD (By similarity).
FT   REGION      138    139       Substrate binding (By similarity).
FT   REGION      287    291       Substrate binding (By similarity).
FT   ACT_SITE    414    414       Proton acceptor (By similarity).
FT   BINDING     186    186       FAD (By similarity).
FT   BINDING     186    186       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     294    294       Substrate (By similarity).
FT   BINDING     416    416       FAD (By similarity).
FT   BINDING     434    434       FAD; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   438 AA;  48382 MW;  7220D91CD65F263E CRC64;
     MALRGVSVQL LSRVPGLRVF RTWVSSAAQT EKVGRTQSQL AKSSRPEFDW RDPLVLEEQL
     TTDEILIRDT FRTYCQERLM PRILLANRNE VFHREIISQM GELGVLGPTI KGYGCAGVSS
     VAYGLLAREL ERVDSGYRSA MSVQSPLVMH PIYAYGSEEQ RQKYLPRLAK GELLGCFGLT
     EPNSGSDPSS METRARYNSS NKSYTLNGTK TWITNSPMAD LFVVWARCED GRIRGFLLEK
     GMRGLSAPRI QGKFSLRASA TGMIIMDGVE VPEENMLPGA SSLGGSFGCL NNGRYGIAWG
     VLGASEFCLH TARQYALDRM QFGVPLARNQ LIQKKLADML TEITLGLHAC LQLGRLKDQD
     KAAPEMVSLL KRNNCGKALD IARQARDMLG GNGISDEYHV IRHAMNLEAV NTYEGTHDIH
     ALILGRAITG IQAFTASK
//