ACADS_RAT
ID ACADS_RAT Reviewed; 412 AA.
AC P15651;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Short-chain specific acyl-CoA dehydrogenase, mitochondrial;
DE Short=SCAD;
DE EC=1.3.8.1 {ECO:0000269|PubMed:3968063};
DE AltName: Full=Butyryl-CoA dehydrogenase;
DE Flags: Precursor;
GN Name=Acads;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-51; 235-250; 314-325
RP AND 350-379.
RX PubMed=2777793; DOI=10.1016/s0021-9258(18)71624-4;
RA Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J.,
RA Ikeda Y., Kraus J., Tanaka K.;
RT "Molecular cloning and nucleotide sequence of cDNAs encoding the precursors
RT of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and
RT isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of
RT the acyl-CoA dehydrogenase family.";
RL J. Biol. Chem. 264:16321-16331(1989).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND PATHWAY.
RX PubMed=3968063; DOI=10.1016/s0021-9258(20)71245-7;
RA Ikeda Y., Okamura-Ikeda K., Tanaka K.;
RT "Purification and characterization of short-chain, medium-chain, and long-
RT chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the
RT holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme.";
RL J. Biol. Chem. 260:1311-1325(1985).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 25-412 IN COMPLEX WITH THE
RP SUBSTRATE ANALOG ACETOACETYL-COA AND FAD, COFACTOR, SUBUNIT, AND ACTIVE
RP SITE.
RX PubMed=11812788; DOI=10.1074/jbc.m111296200;
RA Battaile K.P., Molin-Case J., Paschke R., Wang M., Bennett D., Vockley J.,
RA Kim J.-J.P.;
RT "Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with
RT acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases.";
RL J. Biol. Chem. 277:12200-12207(2002).
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
CC (PubMed:3968063). The first step of fatty acid beta-oxidation consists
CC in the removal of one hydrogen from C-2 and C-3 of the straight-chain
CC fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-
CC CoA (PubMed:3968063). Among the different mitochondrial acyl-CoA
CC dehydrogenases, short-chain specific acyl-CoA dehydrogenase acts
CC specifically on acyl-CoAs with saturated 4 to 6 carbons long primary
CC chains (PubMed:3968063). {ECO:0000269|PubMed:3968063,
CC ECO:0000303|PubMed:3968063}.
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:3968063};
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:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24005;
CC Evidence={ECO:0000305|PubMed:3968063};
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:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43457;
CC Evidence={ECO:0000305|PubMed:3968063};
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:3968063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43465;
CC Evidence={ECO:0000305|PubMed:3968063};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11812788, ECO:0000269|PubMed:3968063};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11812788,
CC ECO:0000269|PubMed:3968063};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.7 uM for butanoyl-CoA {ECO:0000269|PubMed:3968063};
CC KM=32.9 uM for pentanoyl-CoA {ECO:0000269|PubMed:3968063};
CC KM=285 uM for hexanoyl-CoA {ECO:0000269|PubMed:3968063};
CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation.
CC {ECO:0000305|PubMed:3968063}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11812788,
CC ECO:0000269|PubMed:3968063}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q3ZBF6}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40669.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J05030; AAA40669.1; ALT_INIT; mRNA.
DR PIR; B34252; B34252.
DR RefSeq; NP_071957.1; NM_022512.2.
DR PDB; 1JQI; X-ray; 2.25 A; A/B=25-412.
DR PDBsum; 1JQI; -.
DR AlphaFoldDB; P15651; -.
DR SMR; P15651; -.
DR BioGRID; 249019; 3.
DR IntAct; P15651; 15.
DR STRING; 10116.ENSRNOP00000001556; -.
DR ChEMBL; CHEMBL2176825; -.
DR CarbonylDB; P15651; -.
DR iPTMnet; P15651; -.
DR PhosphoSitePlus; P15651; -.
DR jPOST; P15651; -.
DR PaxDb; P15651; -.
DR PRIDE; P15651; -.
DR GeneID; 64304; -.
DR KEGG; rno:64304; -.
DR UCSC; RGD:620514; rat.
DR CTD; 35; -.
DR RGD; 620514; Acads.
DR eggNOG; KOG0139; Eukaryota.
DR InParanoid; P15651; -.
DR OrthoDB; 589058at2759; -.
DR BRENDA; 1.3.8.1; 5301.
DR Reactome; R-RNO-77350; Beta oxidation of hexanoyl-CoA to butanoyl-CoA.
DR Reactome; R-RNO-77352; Beta oxidation of butanoyl-CoA to acetyl-CoA.
DR SABIO-RK; P15651; -.
DR UniPathway; UPA00660; -.
DR EvolutionaryTrace; P15651; -.
DR PRO; PR:P15651; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:BHF-UCL.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IDA:RGD.
DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IDA:RGD.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:RGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0046359; P:butyrate catabolic process; IDA:RGD.
DR GO; GO:0006635; P:fatty acid beta-oxidation; TAS:RGD.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
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 3D-structure; Acetylation; Direct protein sequencing; FAD;
KW Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2777793"
FT CHAIN 25..412
FT /note="Short-chain specific acyl-CoA dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000000501"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:11812788"
FT BINDING 152..161
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11812788"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11812788"
FT BINDING 185..187
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11812788"
FT BINDING 269..272
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11812788"
FT BINDING 297
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11812788"
FT BINDING 365..369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11812788"
FT BINDING 394..396
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11812788"
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 292
FT /note="N6-acetyllysine"
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"
FT HELIX 36..52
FT /evidence="ECO:0007829|PDB:1JQI"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:1JQI"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 174..187
FT /evidence="ECO:0007829|PDB:1JQI"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 238..249
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 260..296
FT /evidence="ECO:0007829|PDB:1JQI"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 308..336
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 342..367
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:1JQI"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:1JQI"
FT HELIX 395..410
FT /evidence="ECO:0007829|PDB:1JQI"
SQ SEQUENCE 412 AA; 44765 MW; 3E4A052FC99B8E14 CRC64;
MAAALLARAG GSLGRALRAR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE KELVPIAAQL
DKEHLFPTSQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI ALEEISRGCA STGVIMSVNN
SLYLGPILKF GSSQQKQQWI TPFTNGDKIG CFALSEPGNG SDAGAASTTA REEGDSWVLN
GTKAWITNSW EASATVVFAS TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN
LIFEDCRIPK ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRHAF
GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL AASEAATAIS
HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL VIAGHLLRSY RS
