ID ACDS_MEGEL STANDARD; PRT; 383 AA. AC Q06319; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 07-FEB-2006, entry version 39. DE Acyl-CoA dehydrogenase, short-chain specific (EC 1.3.99.2) (SCAD) DE (Butyryl-CoA dehydrogenase) (BCAD). OS Megasphaera elsdenii. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Acidaminococcaceae; OC Megasphaera. OX NCBI_TaxID=907; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-50. RX MEDLINE=94002067; PubMed=8399220; 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 MEDLINE=95161388; PubMed=7857927; 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 + acceptor = 2-butenoyl-CoA + CC reduced acceptor. CC -!- COFACTOR: FAD. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. 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 PDB; 1BUC; X-ray; A/B=1-383. DR LinkHub; Q06319; -. DR InterPro; IPR006089; Acyl-CoA_dh. DR InterPro; IPR006090; Acyl-CoA_dh_C. DR InterPro; IPR006091; Acyl-CoA_dh_M. DR InterPro; IPR006092; Acyl-CoA_dh_N. 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 PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. 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 STRAND 2 2 FT HELIX 7 22 FT TURN 23 27 FT HELIX 28 34 FT TURN 35 35 FT HELIX 39 46 FT TURN 47 48 FT STRAND 49 49 FT HELIX 50 52 FT TURN 53 54 FT STRAND 55 55 FT HELIX 57 59 FT TURN 60 60 FT HELIX 62 65 FT TURN 66 66 FT HELIX 69 82 FT HELIX 84 96 FT TURN 97 97 FT HELIX 98 104 FT HELIX 107 112 FT TURN 113 113 FT HELIX 114 119 FT TURN 120 120 FT STRAND 121 122 FT STRAND 124 127 FT STRAND 130 130 FT TURN 131 132 FT STRAND 133 135 FT HELIX 137 139 FT STRAND 143 146 FT TURN 148 149 FT STRAND 150 150 FT STRAND 152 162 FT TURN 163 166 FT STRAND 168 176 FT STRAND 178 181 FT TURN 182 183 FT STRAND 184 191 FT TURN 192 193 FT TURN 195 196 FT STRAND 197 202 FT STRAND 205 207 FT TURN 209 210 FT STRAND 211 211 FT STRAND 213 223 FT HELIX 225 227 FT STRAND 228 230 FT TURN 232 233 FT STRAND 234 234 FT HELIX 235 271 FT STRAND 273 274 FT TURN 275 276 FT STRAND 277 278 FT HELIX 279 281 FT STRAND 282 282 FT HELIX 283 312 FT TURN 313 313 FT HELIX 317 347 FT STRAND 348 348 FT TURN 349 350 FT STRAND 351 352 FT HELIX 353 364 FT TURN 365 367 FT STRAND 368 368 FT HELIX 370 381 FT TURN 382 382 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 //