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 23-MAY-2018, entry version 97. DE RecName: Full=Acyl-CoA dehydrogenase, short-chain specific; DE EC=1.3.8.1; DE AltName: Full=Butyryl-CoA dehydrogenase; DE Short=BCAD; DE AltName: Full=SCAD; OS Megasphaera elsdenii. OC Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae; OC Megasphaera. OX NCBI_TaxID=907; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-50. RX PubMed=8399220; DOI=10.1021/bi00091a026; RA Becker D.F., Fuchs J.A., Banfield D.K., Funk W.D., RA Macgillivray R.T.A., Stankovich M.T.; RT "Characterization of wild-type and an active-site mutant in RT Escherichia coli of short-chain acyl-CoA dehydrogenase from RT 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 RT Megasphaera elsdenii."; RL Biochemistry 34:2163-2171(1995). CC -!- FUNCTION: Has an optimum specificity for 4-carbon length fatty CC acyl-CoAs. CC -!- CATALYTIC ACTIVITY: Butanoyl-CoA + electron-transfer flavoprotein CC = 2-butenoyl-CoA + reduced electron-transfer flavoprotein. CC -!- CATALYTIC ACTIVITY: A short-chain acyl-CoA + electron-transfer CC flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced CC electron-transfer flavoprotein. {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 ProteinModelPortal; Q06319; -. DR SMR; Q06319; -. DR DrugBank; DB03059; Acetoacetyl-Coenzyme A. DR DrugBank; DB03147; Flavin adenine dinucleotide. DR GeneID; 36311878; -. DR eggNOG; ENOG4105C1G; Bacteria. DR eggNOG; COG1960; LUCA. DR BioCyc; MetaCyc:MONOMER-11937; -. DR EvolutionaryTrace; Q06319; -. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro. 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 Gene3D; 1.10.540.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. 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; Direct protein sequencing; FAD; Fatty acid metabolism; KW Flavoprotein; Lipid metabolism; Oxidoreductase. FT CHAIN 1 383 Acyl-CoA dehydrogenase, short-chain FT specific. FT /FTId=PRO_0000201190. FT ACT_SITE 367 367 Proton acceptor. FT MUTAGEN 367 367 E->Q: Loss of activity. FT HELIX 7 22 {ECO:0000244|PDB:1BUC}. FT TURN 23 27 {ECO:0000244|PDB:1BUC}. FT HELIX 28 34 {ECO:0000244|PDB:1BUC}. FT HELIX 39 46 {ECO:0000244|PDB:1BUC}. FT HELIX 50 52 {ECO:0000244|PDB:1BUC}. FT HELIX 57 59 {ECO:0000244|PDB:1BUC}. FT HELIX 62 65 {ECO:0000244|PDB:1BUC}. FT HELIX 69 82 {ECO:0000244|PDB:1BUC}. FT HELIX 84 96 {ECO:0000244|PDB:1BUC}. FT HELIX 98 104 {ECO:0000244|PDB:1BUC}. FT HELIX 107 112 {ECO:0000244|PDB:1BUC}. FT HELIX 114 119 {ECO:0000244|PDB:1BUC}. FT STRAND 124 127 {ECO:0000244|PDB:1BUC}. FT STRAND 133 135 {ECO:0000244|PDB:1BUC}. FT HELIX 137 139 {ECO:0000244|PDB:1BUC}. FT STRAND 143 146 {ECO:0000244|PDB:1BUC}. FT STRAND 152 162 {ECO:0000244|PDB:1BUC}. FT TURN 163 166 {ECO:0000244|PDB:1BUC}. FT STRAND 168 176 {ECO:0000244|PDB:1BUC}. FT STRAND 178 181 {ECO:0000244|PDB:1BUC}. FT STRAND 184 191 {ECO:0000244|PDB:1BUC}. FT STRAND 197 202 {ECO:0000244|PDB:1BUC}. FT STRAND 213 223 {ECO:0000244|PDB:1BUC}. FT HELIX 225 227 {ECO:0000244|PDB:1BUC}. FT STRAND 228 230 {ECO:0000244|PDB:1BUC}. FT HELIX 235 271 {ECO:0000244|PDB:1BUC}. FT HELIX 279 281 {ECO:0000244|PDB:1BUC}. FT HELIX 283 312 {ECO:0000244|PDB:1BUC}. FT HELIX 317 342 {ECO:0000244|PDB:1BUC}. FT HELIX 343 347 {ECO:0000244|PDB:1BUC}. FT HELIX 353 360 {ECO:0000244|PDB:1BUC}. FT HELIX 361 364 {ECO:0000244|PDB:1BUC}. FT TURN 365 367 {ECO:0000244|PDB:1BUC}. FT HELIX 370 381 {ECO:0000244|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 //