ID ACDS_MEGEL STANDARD; PRT; 383 AA. AC Q06319; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Acyl-CoA dehydrogenase, short-chain specific (EC 1.3.99.2) DE (SCAD) (Butyryl-CoA dehydrogenase) (BCAD). OS Megasphaera elsdenii. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Acidaminococcaceae; OC Megasphaera. OX NCBI_TaxID=907; RN [1] RP SEQUENCE FROM N.A., AND 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 + ETF = 2-butenoyl-CoA + reduced CC ETF. 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; -. DR PDB; 1BUC; 20-APR-95. 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. 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 Oxidoreductase; Flavoprotein; FAD; Fatty acid metabolism; KW 3D-structure. FT ACT_SITE 367 367 BASE. 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 HELIX 50 52 FT TURN 53 54 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 124 127 FT STRAND 130 130 FT TURN 131 132 FT STRAND 133 133 FT HELIX 137 139 FT STRAND 143 146 FT TURN 148 149 FT STRAND 152 162 FT TURN 163 166 FT STRAND 169 175 FT TURN 182 183 FT STRAND 185 191 FT TURN 192 193 FT TURN 195 196 FT STRAND 197 202 FT TURN 209 210 FT STRAND 213 223 FT HELIX 225 227 FT STRAND 228 229 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 HELIX 283 312 FT TURN 313 313 FT HELIX 317 342 FT HELIX 343 347 FT TURN 349 350 FT HELIX 353 360 FT HELIX 361 364 FT TURN 365 367 FT HELIX 370 381 FT TURN 382 383 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 //