ACDSB_PONAB
ID ACDSB_PONAB Reviewed; 432 AA.
AC Q5RF40;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial {ECO:0000250|UniProtKB:P70584};
DE Short=SBCAD {ECO:0000250|UniProtKB:P70584};
DE EC=1.3.8.5 {ECO:0000250|UniProtKB:P70584};
DE AltName: Full=2-methyl branched chain acyl-CoA dehydrogenase;
DE Short=2-MEBCAD;
DE AltName: Full=2-methylbutyryl-coenzyme A dehydrogenase;
DE Short=2-methylbutyryl-CoA dehydrogenase;
DE Flags: Precursor;
GN Name=ACADSB;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Short and branched chain specific acyl-CoA dehydrogenase that
CC catalyzes the removal of one hydrogen from C-2 and C-3 of the fatty
CC acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA.
CC Among the different mitochondrial acyl-CoA dehydrogenases, acts
CC specifically on short and branched chain acyl-CoA derivatives such as
CC (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such
CC as butyryl-CoA (By similarity). Plays an important role in the
CC metabolism of L-isoleucine by catalyzing the dehydrogenation of 2-
CC methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic
CC pathway (By similarity). Can also act on valproyl-CoA, a metabolite of
CC the valproic acid drug (By similarity). {ECO:0000250|UniProtKB:P45954,
CC ECO:0000250|UniProtKB:P70584}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:43780, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57336,
CC ChEBI:CHEBI:57337, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.5;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43781;
CC Evidence={ECO:0000250|UniProtKB:P70584};
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:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48257;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = ethylacryloyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:65296, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:156439, ChEBI:CHEBI:156440;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65297;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:24004, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58307;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24005;
CC Evidence={ECO:0000250|UniProtKB:P70584};
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:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44181;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:43464, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:62077, ChEBI:CHEBI:62620;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] + valproyl-
CC CoA = (2E)-2-propylpent-2-enoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:65344, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:156457, ChEBI:CHEBI:156458;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65345;
CC Evidence={ECO:0000250|UniProtKB:P70584};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P45954};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000250|UniProtKB:P45954}.
CC -!- PATHWAY: Amino-acid degradation; L-isoleucine degradation.
CC {ECO:0000250|UniProtKB:P45954}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P45954}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P45954}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CR857321; CAH89617.1; -; mRNA.
DR RefSeq; NP_001124722.1; NM_001131250.1.
DR AlphaFoldDB; Q5RF40; -.
DR SMR; Q5RF40; -.
DR STRING; 9601.ENSPPYP00000003189; -.
DR GeneID; 100171571; -.
DR KEGG; pon:100171571; -.
DR CTD; 36; -.
DR eggNOG; KOG0139; Eukaryota.
DR InParanoid; Q5RF40; -.
DR OrthoDB; 589058at2759; -.
DR UniPathway; UPA00364; -.
DR UniPathway; UPA00660; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0047119; F:2-methyl-branched-chain-enoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0003853; F:2-methylacyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0102035; F:isobutyryl-CoA:FAD oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016937; F:short-branched-chain-acyl-CoA dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0006550; P:isoleucine catabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Mitochondrion; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT CHAIN 34..432
FT /note="Short/branched chain specific acyl-CoA
FT dehydrogenase, mitochondrial"
FT /id="PRO_0000330465"
FT ACT_SITE 414
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 174..183
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:P45954"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 207..209
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:P45954"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 291..294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 319
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 330
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 387..391
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT BINDING 416..418
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:P45954"
FT MOD_RES 70
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBL1"
FT MOD_RES 70
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBL1"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT MOD_RES 284
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P45954"
FT MOD_RES 284
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBL1"
FT MOD_RES 426
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBL1"
SQ SEQUENCE 432 AA; 47485 MW; 09BB4B21ED945736 CRC64;
MEGLAVRLLR GSRLLRRNFP TCLSSWKIPP HVSKSSQSEA LLNITNNGIH FAPLQTFTDE
EMMIKSSVKK FAQEQIAPLV STMDENSKME KSVIQGLFQQ GLMGIEVDPE YGGTGASFLS
TVLVIEELAK VDASVAVFCE IQNTLINTLI RKHGTEEQKG TYLPQLTTEK VGSFCLSEAG
AGSDSFALKT RADKEGDYYV LNGSKMWISS AEHAGLFLVM ANVDPTIGYK GITSFLVDRD
TPGLHIGKPE NKLGLRASST CPLTFENVKV PETNILGQIG HGYKYAIGSL NEGRIGIAAQ
MLGLAQGCFD YTIPYIKERI QFGKRLFDFQ GLQHQVAHVA TQLEAARLLT YNAARLLEAG
KPFIKEASMA KYYASEIAGQ TTSKCIEWMG GVGYTKDYPV EKYFRDAKIG TIYEGASNIQ
LNTIAKHIDA EY
