ACADS_BOVIN
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 03-AUG-2022, entry version 99.
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.ENSBTAP00000009844; -.
DR PaxDb; Q3ZBF6; -.
DR PeptideAtlas; Q3ZBF6; -.
DR PRIDE; Q3ZBF6; -.
DR GeneID; 511222; -.
DR KEGG; bta:511222; -.
DR CTD; 35; -.
DR eggNOG; KOG0139; Eukaryota.
DR InParanoid; Q3ZBF6; -.
DR OrthoDB; 589058at2759; -.
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 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 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
