ID   ACDS_CLOAB              Reviewed;         379 AA.
AC   P52042;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Acyl-CoA dehydrogenase, short-chain specific;
DE            EC=1.3.8.1;
DE   AltName: Full=Butyryl-CoA dehydrogenase;
DE   AltName: Full=SCAD;
GN   Name=bcd; OrderedLocusNames=CA_C2711;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=8655474; DOI=10.1128/jb.178.11.3015-3024.1996;
RA   Boynton Z.L., Bennett G.N., Rudolph F.B.;
RT   "Cloning, sequencing, and expression of clustered genes encoding beta-
RT   hydroxybutyryl-coenzyme A (CoA) dehydrogenase, crotonase, and butyryl-CoA
RT   dehydrogenase from Clostridium acetobutylicum ATCC 824.";
RL   J. Bacteriol. 178:3015-3024(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butanoyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (2E)-butenoyl-CoA + reduced [electron-transfer
CC         flavoprotein]; Xref=Rhea:RHEA:24004, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC         COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57332, ChEBI:CHEBI:57371,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.1;
CC         Evidence={ECO:0000269|PubMed:8655474};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized
CC         [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA +
CC         reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47196,
CC         Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:87487,
CC         ChEBI:CHEBI:87488; EC=1.3.8.1; Evidence={ECO:0000269|PubMed:8655474};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U17110; AAA95968.1; -; Genomic_DNA.
DR   EMBL; AE001437; AAK80657.1; -; Genomic_DNA.
DR   PIR; F97233; F97233.
DR   PIR; T47262; T47262.
DR   RefSeq; NP_349317.1; NC_003030.1.
DR   RefSeq; WP_010965998.1; NC_003030.1.
DR   AlphaFoldDB; P52042; -.
DR   SMR; P52042; -.
DR   STRING; 272562.CA_C2711; -.
DR   PRIDE; P52042; -.
DR   EnsemblBacteria; AAK80657; AAK80657; CA_C2711.
DR   GeneID; 44999200; -.
DR   KEGG; cac:CA_C2711; -.
DR   PATRIC; fig|272562.8.peg.2901; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_9; -.
DR   OMA; NMATWML; -.
DR   OrthoDB; 760677at2; -.
DR   BioCyc; MetaCyc:BCDCLOS-MON; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000000814; Chromosome.
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:InterPro.
DR   GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
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   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..379
FT                   /note="Acyl-CoA dehydrogenase, short-chain specific"
FT                   /id="PRO_0000201189"
SQ   SEQUENCE   379 AA;  41387 MW;  4BC50A1991BD9FB2 CRC64;
     MDFNLTREQE LVRQMVREFA ENEVKPIAAE IDETERFPME NVKKMGQYGM MGIPFSKEYG
     GAGGDVLSYI IAVEELSKVC GTTGVILSAH TSLCASLINE HGTEEQKQKY LVPLAKGEKI
     GAYGLTEPNA GTDSGAQQTV AVLEGDHYVI NGSKIFITNG GVADTFVIFA MTDRTKGTKG
     ISAFIIEKGF KGFSIGKVEQ KLGIRASSTT ELVFEDMIVP VENMIGKEGK GFPIAMKTLD
     GGRIGIAAQA LGIAEGAFNE ARAYMKERKQ FGRSLDKFQG LAWMMADMDV AIESARYLVY
     KAAYLKQAGL PYTVDAARAK LHAANVAMDV TTKAVQLFGG YGYTKDYPVE RMMRDAKITE
     IYEGTSEVQK LVISGKIFR