GCDH_CAEEL
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 03-AUG-2022, entry version 146.
DE RecName: Full=Probable glutaryl-CoA dehydrogenase, mitochondrial;
DE Short=GCD;
DE EC=1.3.8.6;
DE Flags: Precursor;
GN ORFNames=F54D5.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX 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 investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutaryl-CoA + 2 H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-butenoyl-CoA + CO2 + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:13389, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:57378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.6;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid metabolism; lysine degradation.
CC -!- PATHWAY: Amino-acid metabolism; tryptophan metabolism.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; Z66513; CAA91333.1; -; Genomic_DNA.
DR PIR; T22647; T22647.
DR RefSeq; NP_496469.1; NM_064068.5.
DR AlphaFoldDB; Q20772; -.
DR SMR; Q20772; -.
DR BioGRID; 40074; 8.
DR DIP; DIP-25054N; -.
DR IntAct; Q20772; 3.
DR STRING; 6239.F54D5.7.2; -.
DR EPD; Q20772; -.
DR PaxDb; Q20772; -.
DR PeptideAtlas; Q20772; -.
DR EnsemblMetazoa; F54D5.7.1; F54D5.7.1; WBGene00010052.
DR GeneID; 174768; -.
DR UCSC; F54D5.7.1; c. elegans.
DR CTD; 174768; -.
DR WormBase; F54D5.7; CE03411; WBGene00010052; -.
DR eggNOG; KOG0138; Eukaryota.
DR GeneTree; ENSGT00940000158116; -.
DR HOGENOM; CLU_018204_8_0_1; -.
DR InParanoid; Q20772; -.
DR OMA; AAMDCYD; -.
DR OrthoDB; 589058at2759; -.
DR PhylomeDB; Q20772; -.
DR Reactome; R-CEL-71064; Lysine catabolism.
DR UniPathway; UPA00224; -.
DR UniPathway; UPA00225; -.
DR PRO; PR:Q20772; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00010052; Expressed in larva and 4 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0004361; F:glutaryl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR GO; GO:0046949; P:fatty-acyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0006568; P:tryptophan metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
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 SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..409
FT /note="Probable glutaryl-CoA dehydrogenase, mitochondrial"
FT /id="PRO_0000000530"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 110..111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149..152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184..186
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 261..265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
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
