ID ACDS_MEGEL Reviewed; 383 AA. AC Q06319; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=Acyl-CoA dehydrogenase, short-chain specific; DE EC=1.3.8.1 {ECO:0000269|PubMed:8399220}; DE AltName: Full=Butyryl-CoA dehydrogenase; DE Short=BCAD; DE AltName: Full=SCAD; OS Megasphaera elsdenii. OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=907; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-50, FUNCTION, RP CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF GLU-367. RX PubMed=8399220; DOI=10.1021/bi00091a026; RA Becker D.F., Fuchs J.A., Banfield D.K., Funk W.D., Macgillivray R.T.A., RA Stankovich M.T.; RT "Characterization of wild-type and an active-site mutant in Escherichia RT coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii."; RL Biochemistry 32:10736-10742(1993). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=7857927; DOI=10.1021/bi00007a009; RA Djordjevic S., Pace C.P., Stankovich M.T., Kim J.-J.P.; RT "Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera RT elsdenii."; RL Biochemistry 34:2163-2171(1995). CC -!- FUNCTION: Has an optimum specificity for 4-carbon length fatty acyl- CC CoAs. {ECO:0000269|PubMed:8399220}. 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:8399220}; 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; CC Evidence={ECO:0000250|UniProtKB:P52042}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC {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; L04528; AAA03594.1; -; Unassigned_DNA. DR RefSeq; WP_014017064.1; NZ_NQMW01000006.1. DR PDB; 1BUC; X-ray; 2.50 A; A/B=1-383. DR PDBsum; 1BUC; -. DR AlphaFoldDB; Q06319; -. DR SMR; Q06319; -. DR DrugBank; DB03059; Acetoacetyl-CoA. DR DrugBank; DB03147; Flavin adenine dinucleotide. DR GeneID; 69665179; -. DR OrthoDB; 9802447at2; -. DR BioCyc; MetaCyc:MONOMER-11937; -. DR EvolutionaryTrace; Q06319; -. DR GO; GO:0004085; F:butyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. 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:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 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; Direct protein sequencing; FAD; Fatty acid metabolism; KW Flavoprotein; Lipid metabolism; Oxidoreductase. FT CHAIN 1..383 FT /note="Acyl-CoA dehydrogenase, short-chain specific" FT /id="PRO_0000201190" FT ACT_SITE 367 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:8399220" FT MUTAGEN 367 FT /note="E->Q: Loss of activity." FT /evidence="ECO:0000269|PubMed:8399220" FT HELIX 7..22 FT /evidence="ECO:0007829|PDB:1BUC" FT TURN 23..27 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 28..34 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 39..46 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 50..52 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 62..65 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 69..82 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 84..96 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 98..104 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 107..112 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 114..119 FT /evidence="ECO:0007829|PDB:1BUC" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:1BUC" FT STRAND 133..135 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:1BUC" FT STRAND 143..146 FT /evidence="ECO:0007829|PDB:1BUC" FT STRAND 152..162 FT /evidence="ECO:0007829|PDB:1BUC" FT TURN 163..166 FT /evidence="ECO:0007829|PDB:1BUC" FT STRAND 168..176 FT /evidence="ECO:0007829|PDB:1BUC" FT STRAND 178..181 FT /evidence="ECO:0007829|PDB:1BUC" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:1BUC" FT STRAND 197..202 FT /evidence="ECO:0007829|PDB:1BUC" FT STRAND 213..223 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:1BUC" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 235..271 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 279..281 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 283..312 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 317..342 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 343..347 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 353..360 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 361..364 FT /evidence="ECO:0007829|PDB:1BUC" FT TURN 365..367 FT /evidence="ECO:0007829|PDB:1BUC" FT HELIX 370..381 FT /evidence="ECO:0007829|PDB:1BUC" SQ SEQUENCE 383 AA; 41408 MW; 3D68AAE34D9BBAB8 CRC64; MDFNLTDIQQ DFLKLAHDFG EKKLAPTVTE RDHKGIYDKE LIDELLSLGI TGAYFEEKYG GSGDDGGDVL SYILAVEELA KYDAGVAITL SATVSLCANP IWQFGTEAQK EKFLVPLVEG TKLGAFGLTE PNAGTDASGQ QTIATKNDDG TYTLNGSKIF ITNGGAADIY IVFAMTDKSK GNHGITAFIL EDGTPGFTYG KKEDKMGIHT SQTMELVFQD VKVPAENMLG EEGKGFKIAM MTLDGGRIGV AAQALGIAEA ALADAVEYSK QRVQFGKPLC KFQSISFKLA DMKMQIEAAR NLVYKAACKK QEGKPFTVDA AIAKRVASDV AMRVTTEAVQ IFGGYGYSEE YPVARHMRDA KITQIYEGTN EVQLMVTGGA LLR //