ID   GCDH_DICDI              Reviewed;         420 AA.
AC   Q54R47;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   16-JUN-2009, entry version 37.
DE   RecName: Full=Glutaryl-CoA dehydrogenase, mitochondrial;
DE            Short=GCD;
DE            EC=1.3.99.7;
DE   Flags: Precursor;
GN   Name=gcdh; ORFNames=DDB_G0283411;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (Potential).
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
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DR   EMBL; AAFI02000055; EAL65690.1; -; Genomic_DNA.
DR   RefSeq; XP_639044.1; -.
DR   GeneID; 3390655; -.
DR   KEGG; ddi:DDB_0234151; -.
DR   dictyBase; DDB_G0283411; gcdh.
DR   OMA; Q54R47; CFETARE.
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   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    420       Glutaryl-CoA dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000330829.
FT   NP_BIND     164    167       FAD (By similarity).
FT   NP_BIND     198    200       FAD (By similarity).
FT   REGION      125    126       Substrate binding (By similarity).
FT   REGION      273    277       Substrate binding (By similarity).
FT   ACT_SITE    400    400       Proton acceptor (By similarity).
FT   BINDING     173    173       FAD (By similarity).
FT   BINDING     173    173       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     280    280       Substrate (By similarity).
FT   BINDING     402    402       FAD (By similarity).
FT   BINDING     420    420       FAD; via carboxyl oxygen (By similarity).
SQ   SEQUENCE   420 AA;  45875 MW;  659A877F3251AF6E CRC64;
     MLSNLSKSLL SKGKFINKNN LLKNKRSFGT IVPGDKFEWN DPLSLESLLT EEEVMIRDQV
     NKFCQDELMP RIQMAYRDEK FDREIMREYG KMGMLGATIP AYGGVSHVAY GLMANAVEKV
     DSGYRSAMSV QSSLVMHPIN TFGTDAQKSK YLDGLASGDL VGCFGLTEPN AGSDPAGMQT
     RAVKNSAGNY VLNGTKTWIT NSPIADVFVV WAKVENGDIR GFVLEKGMKG LSAPKIEGKL
     SLRASITGMI VMEDVEVPPT AMFPEVKGLR GPFSCLNKAR YGIGWGSLGA AEFCYSTARQ
     YGLDRKQFGK PLAANQLYQK KLADMATEIS LGLQACYQVG RLIDAGKATP ERISLIKRNS
     CGKSLDIARQ SRDMLGGNGI ADEYHVIRHA ANLETVNTYE GTHDIHALIL GRAITGIPSF
//