ID   GCDH_CAEEL              Reviewed;         409 AA.
AC   Q20772;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Probable glutaryl-CoA dehydrogenase, mitochondrial;
DE            Short=GCD;
DE            EC=1.3.99.7;
DE   Flags: Precursor;
GN   ORFNames=F54D5.7;
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   -!- 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   -!- INTERACTION:
CC       P39745:mpk-1; NbExp=1; IntAct=EBI-313068, EBI-321013;
CC       Q17446:pmk-1; NbExp=1; IntAct=EBI-313068, EBI-312987;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (Potential).
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; Z66513; CAA91333.1; -; Genomic_DNA.
DR   PIR; T22647; T22647.
DR   RefSeq; NP_496469.1; -.
DR   UniGene; Cel.30446; -.
DR   HSSP; Q06319; 1BUC.
DR   DIP; DIP:25054N; -.
DR   IntAct; Q20772; 6.
DR   Ensembl; F54D5.7; Caenorhabditis elegans.
DR   GeneID; 174768; -.
DR   KEGG; cel:F54D5.7; -.
DR   WormBase; WBGene00010052; F54D5.7.
DR   WormPep; F54D5.7; CE03411.
DR   OMA; Q20772; CFETARE.
DR   BRENDA; 1.3.99.7; 672.
DR   NextBio; 885416; -.
DR   ArrayExpress; Q20772; -.
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:0005515; F:protein binding; IPI:IntAct.
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; FALSE_NEG.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    409       Probable glutaryl-CoA dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000000530.
FT   NP_BIND     149    152       FAD (By similarity).
FT   NP_BIND     184    186       FAD (By similarity).
FT   REGION      110    111       Substrate binding (By similarity).
FT   REGION      261    265       Substrate binding (By similarity).
FT   ACT_SITE    388    388       Proton acceptor (By similarity).
FT   BINDING     158    158       FAD (By similarity).
FT   BINDING     158    158       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     268    268       Substrate (By similarity).
FT   BINDING     390    390       FAD (By similarity).
FT   BINDING     408    408       FAD; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   409 AA;  44964 MW;  4D06241FB6768069 CRC64;
     MLTRGFTSIG KIASRGLSST FYQDAFQLSD QLTEDERSLM LSAREYCQER LLPRVTEAYR
     TEKFDPSLIP EMGSMGLLGA PYQGYGCAGT STVGYGLIAR EVERVDSGYR STMSVQTSLV
     IGPIYNYGSE DQKQKYIPDL ASGKKIGCFG LTEPNHGSNP GGMETKATWD ETTKTYKLNG
     SKTWISNSPV SDVMVVWARS ARHNNKIKGF ILERGMKGLT TPKIEGKLSL RASITGQIAM
     DDVPVPEENL LPNAEGLQGP FGCLNNARLG IAWGALGAAE ECFHLARQYT LDRQQFGRPL
     AQNQLMQLKM ADMLTEISLG LQGCLRVSRL KDEGKVQSEQ ISIIKRNSCG KALEVARKAR
     DMLGGNGIVD EYHIMRHMVN LETVNTYEGT HDVHALILGR AITGLNGFC
//