GCDH_DICDI
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 03-AUG-2022, entry version 107.
DE RecName: Full=Glutaryl-CoA dehydrogenase, mitochondrial;
DE Short=GCD;
DE EC=1.3.8.6;
DE Flags: Precursor;
GN Name=gcdh; ORFNames=DDB_G0283411;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; 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., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., 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., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000055; EAL65690.1; -; Genomic_DNA.
DR RefSeq; XP_639044.1; XM_633952.1.
DR AlphaFoldDB; Q54R47; -.
DR SMR; Q54R47; -.
DR STRING; 44689.DDB0234151; -.
DR PaxDb; Q54R47; -.
DR EnsemblProtists; EAL65690; EAL65690; DDB_G0283411.
DR GeneID; 8624069; -.
DR KEGG; ddi:DDB_G0283411; -.
DR dictyBase; DDB_G0283411; gcdh.
DR eggNOG; KOG0138; Eukaryota.
DR HOGENOM; CLU_018204_8_0_1; -.
DR InParanoid; Q54R47; -.
DR OMA; AAMDCYD; -.
DR PhylomeDB; Q54R47; -.
DR Reactome; R-DDI-71064; Lysine catabolism.
DR UniPathway; UPA00224; -.
DR UniPathway; UPA00225; -.
DR PRO; PR:Q54R47; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
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; PS00072; ACYL_COA_DH_1; 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 ?..420
FT /note="Glutaryl-CoA dehydrogenase, mitochondrial"
FT /id="PRO_0000330829"
FT ACT_SITE 400
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 125..126
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164..167
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198..200
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 273..277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
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
