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 01-NOV-1997 (Rel. 35, 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; Bacillus/Clostridium group; Sporomusa subbranch; OC Megasphaera. RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 1-50. RX MEDLINE; 94002067. 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. 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 DEHYDROGENASES FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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 PFAM; PF00441; Acyl-CoA_dh; 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. SQ SEQUENCE 383 AA; 41408 MW; 4A0C96FE CRC32; 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 //