ID   ACADS_BOVIN             Reviewed;         412 AA.
AC   Q3ZBF6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Short-chain specific acyl-CoA dehydrogenase, mitochondrial;
DE            Short=SCAD;
DE            EC=1.3.8.1 {ECO:0000269|PubMed:6712627};
DE   AltName: Full=Butyryl-CoA dehydrogenase;
DE   Flags: Precursor;
GN   Name=ACADS;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, SUBCELLULAR LOCATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=6712627; DOI=10.1042/bj2180511;
RA   Shaw L., Engel P.C.;
RT   "The purification and properties of ox liver short-chain acyl-CoA
RT   dehydrogenase.";
RL   Biochem. J. 218:511-520(1984).
CC   -!- FUNCTION: Short-chain specific acyl-CoA dehydrogenase is one of the
CC       acyl-CoA dehydrogenases that catalyze the first step of mitochondrial
CC       fatty acid beta-oxidation, an aerobic process breaking down fatty acids
CC       into acetyl-CoA and allowing the production of energy from fats. The
CC       first step of fatty acid beta-oxidation consists in the removal of one
CC       hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA
CC       thioester, resulting in the formation of trans-2-enoyl-CoA (By
CC       similarity). Among the different mitochondrial acyl-CoA dehydrogenases,
CC       short-chain specific acyl-CoA dehydrogenase acts specifically on acyl-
CC       CoAs with saturated 4 to 6 carbons long primary chains
CC       (PubMed:6712627). {ECO:0000250|UniProtKB:P15651,
CC       ECO:0000269|PubMed:6712627}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC         [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA +
CC         reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47196,
CC         Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:87487,
CC         ChEBI:CHEBI:87488; EC=1.3.8.1; Evidence={ECO:0000269|PubMed:6712627};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47197;
CC         Evidence={ECO:0000305|PubMed:6712627};
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; EC=1.3.8.1;
CC         Evidence={ECO:0000269|PubMed:6712627};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24005;
CC         Evidence={ECO:0000305|PubMed:6712627};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + oxidized [electron-transfer flavoprotein] + pentanoyl-
CC         CoA = (2E)-pentenoyl-CoA + reduced [electron-transfer flavoprotein];
CC         Xref=Rhea:RHEA:43456, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57389, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307, ChEBI:CHEBI:86160;
CC         Evidence={ECO:0000269|PubMed:6712627};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43457;
CC         Evidence={ECO:0000305|PubMed:6712627};
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:0000269|PubMed:6712627};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC         Evidence={ECO:0000305|PubMed:6712627};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:6712627};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P15651};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=90 uM for propanoyl-CoA {ECO:0000269|PubMed:6712627};
CC         KM=3 uM for butanoyl-CoA {ECO:0000269|PubMed:6712627};
CC         KM=10 uM for pentanoyl-CoA {ECO:0000269|PubMed:6712627};
CC         KM=22 uM for hexanoyl-CoA {ECO:0000269|PubMed:6712627};
CC         KM=31 uM for heptanoyl-CoA {ECO:0000269|PubMed:6712627};
CC         KM=29 uM for octanoyl-CoA {ECO:0000269|PubMed:6712627};
CC       pH dependence:
CC         Optimum pH is 7.1. {ECO:0000269|PubMed:6712627};
CC   -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC       {ECO:0000250|UniProtKB:P16219}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:6712627}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:6712627}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; BC103365; AAI03366.1; -; mRNA.
DR   RefSeq; NP_001029573.1; NM_001034401.2.
DR   AlphaFoldDB; Q3ZBF6; -.
DR   SMR; Q3ZBF6; -.
DR   STRING; 9913.ENSBTAP00000058080; -.
DR   PaxDb; 9913-ENSBTAP00000009844; -.
DR   PeptideAtlas; Q3ZBF6; -.
DR   GeneID; 511222; -.
DR   KEGG; bta:511222; -.
DR   CTD; 35; -.
DR   eggNOG; KOG0139; Eukaryota.
DR   InParanoid; Q3ZBF6; -.
DR   OrthoDB; 275353at2759; -.
DR   SABIO-RK; Q3ZBF6; -.
DR   UniPathway; UPA00660; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046359; P:butyrate catabolic process; IBA:GO_Central.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR   CDD; cd01158; SCAD_SBCAD; 1.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 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_sf.
DR   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF42; SHORT-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW   Mitochondrion; Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250|UniProtKB:P15651"
FT   CHAIN           25..412
FT                   /note="Short-chain specific acyl-CoA dehydrogenase,
FT                   mitochondrial"
FT                   /id="PRO_0000281994"
FT   ACT_SITE        392
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P15651"
FT   BINDING         152..161
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:P15651"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15651"
FT   BINDING         185..187
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:P15651"
FT   BINDING         269..272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15651"
FT   BINDING         297
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P15651"
FT   BINDING         308
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"
FT   BINDING         365..369
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:P15651"
FT   BINDING         393
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P15651"
FT   BINDING         394..396
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:P15651"
FT   MOD_RES         27
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07417"
FT   MOD_RES         51
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q07417"
FT   MOD_RES         51
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q07417"
FT   MOD_RES         72
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07417"
FT   MOD_RES         129
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q07417"
FT   MOD_RES         129
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q07417"
FT   MOD_RES         208
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07417"
FT   MOD_RES         262
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q07417"
FT   MOD_RES         262
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q07417"
FT   MOD_RES         306
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q07417"
FT   MOD_RES         306
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q07417"
SQ   SEQUENCE   412 AA;  44552 MW;  3845B25B0DEF5265 CRC64;
     MAATLLARAC GLVRGAPWPW GWRRLHTVYQ SVELPETHQM LRQTCRDFAE KELFPIAAQV
     DKEHRFPAAQ VKKMGELGLM AMNVPEELSG AGLDYLAYSI AMEEISRGCA STGVIMSVNN
     SLYLGPILKF GTKEQKQQWV APFTSGDKIG CFALSEPGNG SDAGAAATTA RADGDSWVLS
     GTKAWITNAW EASAVVVFAS TDRSLHNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN
     LIFEDRRIPK DSLLGEPGLG FKIAMQTLDT GRIGIASQAL GIAQAALDCA VTYAENRSAF
     GAPLTKLQAI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKEAAMAKL AASEAATAIT
     HQAMQILGGM GYVKEMPAER HYRDARITEI YEGTSEIQRL VVAGHLLKSY RS
//