ACAD8_DICDI
ID ACAD8_DICDI Reviewed; 416 AA.
AC Q54IM8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Isobutyryl-CoA dehydrogenase, mitochondrial;
DE EC=1.3.8.- {ECO:0000250|UniProtKB:Q9UKU7};
DE AltName: Full=Acyl-CoA dehydrogenase family member 8 homolog;
DE Flags: Precursor;
GN Name=acad8; ORFNames=DDB_G0288647;
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 -!- FUNCTION: Isobutyryl-CoA dehydrogenase which catalyzes one of the steps
CC of the valine catabolic pathway. To a lesser extent, is also able to
CC catalyze the oxidation of (2S)-2-methylbutanoyl-CoA.
CC {ECO:0000250|UniProtKB:Q9UKU7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylpropanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-2-methylpropenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:44180, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57338,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:62500;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44181;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:48256, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57337,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:88166;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48257;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + propanoyl-
CC CoA = acryloyl-CoA + reduced [electron-transfer flavoprotein];
CC Xref=Rhea:RHEA:31287, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57367, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31288;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9UKU7};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC {ECO:0000250|UniProtKB:Q9UKU7}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9UKU7}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9UKU7}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000119; EAL63127.1; -; Genomic_DNA.
DR RefSeq; XP_636630.1; XM_631538.1.
DR AlphaFoldDB; Q54IM8; -.
DR SMR; Q54IM8; -.
DR STRING; 44689.DDB0237710; -.
DR PaxDb; Q54IM8; -.
DR EnsemblProtists; EAL63127; EAL63127; DDB_G0288647.
DR GeneID; 8626731; -.
DR KEGG; ddi:DDB_G0288647; -.
DR dictyBase; DDB_G0288647; acad8.
DR eggNOG; KOG0140; Eukaryota.
DR HOGENOM; CLU_018204_0_2_1; -.
DR InParanoid; Q54IM8; -.
DR OMA; NMATWML; -.
DR PhylomeDB; Q54IM8; -.
DR Reactome; R-DDI-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00362; -.
DR PRO; PR:Q54IM8; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01162; IBD; 1.
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 InterPro; IPR034178; IBD.
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 Activator; Branched-chain amino acid catabolism; FAD; Flavoprotein;
KW Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..416
FT /note="Isobutyryl-CoA dehydrogenase, mitochondrial"
FT /id="PRO_0000328143"
FT ACT_SITE 397
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 156..165
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 189..191
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 273..276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 301
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 311..312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 370..374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 399..401
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
FT BINDING 409
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UKU7"
SQ SEQUENCE 416 AA; 45694 MW; BCA68ACB4C935C46 CRC64;
MISGLFKLSN KQSVLQNATK LVLQRRTFFN IVPNPSVGLT EDQKQFQSMA LDFAQEKMKP
FAEKWDKEEY FPRDVMREAA ELGFGGIYVR EDVGGSGLSR LDASIIIEAL ASADVSTTAF
ISIHNMCAGL IDIYGTEEQR KKFLPSLVSM EKIASYCLTE PGSGSDAGSL STKATKDGDH
YILNGSKAFI SGGGDSEVYL VMVRTGAEKG PKGISCLLVE KDTPGLSFGK KEEKLGWNTQ
PTRALIFEDC RVPVGNLIGK EGQGFSIAMN ALNGGRINIG ACSLGGAQSC LVAARDHVKV
RKQFNQPLEH FQAVQFKMAD MATKLHASRI MIRNAAAMLD AKDPSAHVYI AMAKLFACDE
CFKVTDDSLQ LFGGYGYLKD YPVERYLRDL RVHRILEGSD AVMRLIISRE LSKDDH
