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-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE ACYL-COA DEHYDROGENASE, SHORT-CHAIN SPECIFIC (EC 1.3.99.2) DE (SCAD) (BUTYRYL-COA DEHYDROGENASE). OS MEGASPHAERA ELSDENII. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; ANAEROBIC COCCI; OC VEILLONELLACEAE. RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE; 94002067. RA BECKER D.F., FUCHS J.A., BANFIELD D.K., FUNK W.D., RA MACGILLIVRAY R.T., STANKOVICH M.T.; RL BIOCHEMISTRY 32:10736-10742(1993). CC -!- CATALYTIC ACTIVITY: BUTANOYL-COA + ETF = 2-BUTENOYL-COA + REDUCED CC ETF. CC -!- COFACTOR: FAD FLAVOPROTEIN. CC -!- SIMILARITY: STRONG TO OTHER ACYL-COA DEHYDROGENASES. 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; G149886; -. KW OXIDOREDUCTASE; FLAVOPROTEIN; FAD; FATTY ACID METABOLISM. 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 //