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 27-MAR-2024, entry version 185. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyGen; P15651; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P15651; -. DR PhosphoSitePlus; P15651; -. DR jPOST; P15651; -. DR PaxDb; 10116-ENSRNOP00000001556; -. DR GeneID; 64304; -. DR KEGG; rno:64304; -. DR UCSC; RGD:620514; rat. DR AGR; RGD:620514; -. DR CTD; 35; -. DR RGD; 620514; Acads. DR eggNOG; KOG0139; Eukaryota. DR InParanoid; P15651; -. DR OrthoDB; 275353at2759; -. 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; IBA:GO_Central. 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 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 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 //