ID J7TFF9_CLOS1 Unreviewed; 379 AA. AC J7TFF9; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 07-OCT-2020, entry version 24. DE SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:EDU39342.1}; DE EC=1.3.8.1 {ECO:0000313|EMBL:EDU39342.1}; GN Name=bcd {ECO:0000313|EMBL:EDU39342.1}; GN ORFNames=CLOSPO_00420 {ECO:0000313|EMBL:EDU39342.1}; OS Clostridium sporogenes (strain ATCC 15579). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=471871 {ECO:0000313|EMBL:EDU39342.1, ECO:0000313|Proteomes:UP000006610}; RN [1] {ECO:0000313|Proteomes:UP000006610} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15579 {ECO:0000313|Proteomes:UP000006610}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D., RA Gordon J., Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RT "Draft genome sequence of Clostridium sporogenes ATCC 15579."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|RuleBase:RU362125}; CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EDU39342.1}. 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; ABKW02000002; EDU39342.1; -; Genomic_DNA. DR RefSeq; WP_003483432.1; NZ_DS981517.1. DR EnsemblBacteria; EDU39342; EDU39342; CLOSPO_00420. DR HOGENOM; CLU_018204_0_2_9; -. DR Proteomes; UP000006610; Unassembled WGS sequence. 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:UniProtKB-UniRule. 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 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU362125}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU362125, ECO:0000313|EMBL:EDU39342.1}. FT DOMAIN 6..118 FT /note="Acyl-CoA_dh_N" FT /evidence="ECO:0000259|Pfam:PF02771" FT DOMAIN 122..217 FT /note="Acyl-CoA_dh_M" FT /evidence="ECO:0000259|Pfam:PF02770" FT DOMAIN 229..377 FT /note="Acyl-CoA_dh_1" FT /evidence="ECO:0000259|Pfam:PF00441" SQ SEQUENCE 379 AA; 41685 MW; 90AB967F5A65DF6C CRC64; MEFGLSQEQK LVKQMLMEFV ENEVEPIAAD IDKTERYPIE TVEKMAKYGM MGMPFPKEYG GAGTDYLSYV IAVEELAKEC ATTSVILSAH TSLCCAPIFE FGTEEQKKKY LPDLLSGEKI GAFGLTEPNA GTDASAQQSV AVLEGDHYIL NGSKIFITNG GAADTFVIFA MTDRSKGVRG ISAFILEKEM SGFSIGKTED KMGIRASSTT ELIFEDVKVP KENLLGKEGK GFGIAMKTLD GGRIGIAAQA LGIAEGALDH AVAYMKERKQ FGKNLTKFQG LQWYIADMKV RVEAAKYLVY KSAWKKSTGE NYTMDAAEAK LYAAETAMYV TNKSLQVLGG YGYTKDYPLE RMLRDARITE IYEGTSEVQK MVIANNLLH //