BCD1_SYNWW
ID BCD1_SYNWW Reviewed; 610 AA.
AC Q0AVM4;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Butyryl-CoA dehydrogenase Swol_1933 {ECO:0000303|PubMed:19648244, ECO:0000303|PubMed:23468890};
DE Short=BCD {ECO:0000303|PubMed:19648244, ECO:0000303|PubMed:23468890};
DE EC=1.3.8.1 {ECO:0000269|PubMed:19648244};
GN OrderedLocusNames=Swol_1933 {ECO:0000312|EMBL:ABI69230.1};
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen;
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, INDUCTION, AND PATHWAY.
RX PubMed=19648244; DOI=10.1128/jb.01605-08;
RA Mueller N., Schleheck D., Schink B.;
RT "Involvement of NADH:acceptor oxidoreductase and butyryl coenzyme A
RT dehydrogenase in reversed electron transport during syntrophic butyrate
RT oxidation by Syntrophomonas wolfei.";
RL J. Bacteriol. 191:6167-6177(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, SUBCELLULAR LOCATION,
RP FUNCTION, AND PATHWAY.
RX PubMed=23468890; DOI=10.1371/journal.pone.0056905;
RA Schmidt A., Mueller N., Schink B., Schleheck D.;
RT "A proteomic view at the biochemistry of syntrophic butyrate oxidation in
RT Syntrophomonas wolfei.";
RL PLoS ONE 8:E56905-E56905(2013).
CC -!- FUNCTION: Involved in syntrophic growth of S.wolfei with butyrate, as
CC part of the butyrate oxidation pathway. Catalyzes the oxidation of
CC butanoyl-CoA to crotonyl-CoA. Probably passes the electrons released by
CC this reaction on to electron-transfer flavoproteins (EtfAB) to finally
CC generate hydrogen and/or formate. {ECO:0000269|PubMed:19648244,
CC ECO:0000305|PubMed:23468890}.
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:19648244};
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;
CC Evidence={ECO:0000269|PubMed:19648244};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q2LQP0, ECO:0000305|PubMed:19648244};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC {ECO:0000305|PubMed:19648244, ECO:0000305|PubMed:23468890}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23468890}.
CC -!- INDUCTION: Highly expressed during syntrophic growth with butyrate (at
CC protein level) (PubMed:19648244, PubMed:23468890). Seems to be
CC constitutively expressed (PubMed:23468890).
CC {ECO:0000269|PubMed:19648244, ECO:0000269|PubMed:23468890}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CP000448; ABI69230.1; -; Genomic_DNA.
DR RefSeq; WP_011641323.1; NC_008346.1.
DR AlphaFoldDB; Q0AVM4; -.
DR SMR; Q0AVM4; -.
DR STRING; 335541.Swol_1933; -.
DR EnsemblBacteria; ABI69230; ABI69230; Swol_1933.
DR KEGG; swo:Swol_1933; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_2_9; -.
DR OrthoDB; 357522at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000001968; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR025878; Acyl-CoA_dh-like_C_dom.
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; PF12806; Acyl-CoA_dh_C; 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.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..610
FT /note="Butyryl-CoA dehydrogenase Swol_1933"
FT /id="PRO_0000442211"
FT ACT_SITE 451
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q06319"
SQ SEQUENCE 610 AA; 67830 MW; 7CDF903B7DD0F817 CRC64;
MAHENYLYQM RDIKFAVKEW LDMNKLLSCD AYKDYYGIDD IDAFLDVNFK VCRDVLCPAN
KEADDPGCKF VGGDTQAVIT PEVFKNAYNT VCEAGLGPQF SDRSAEGRMP LVWEAPILEM
QSGASPSIVM FWCLTAGACT VIQHNASEEL KERFLPKMYS GEWGGTMGLT EPGAGSEVGA
VATKCFPTDT PGLYKIKGQK CFITSGDHDL ASNIIHLVLA KTPDAKPGTS GINCLIVPKF
WVNEDGTQGA WNDVTSTGIE HKMGIHGSST LSLSFGENDN CYGWMIGDGP VDGRGKGMAQ
MFQMMNEERL NTGTFAQGCI GSAYYAALDY CKMRVQSPKF TDPKGPSVRI IEHEDVRRML
LFQKSIMEAC RALLYTTYFY QDLSHDAADP AEREYYDDMT MIQIPLCKAY VSDMAWISTE
QAIQCLGGYG FIEEYAPAEL ARDCKIYSLW EGTNFIQAQD FNNRKTTMKK GEPMKKWVAQ
IADFLATKKD PAFADEFAMM DDAFSAYNEI LSTKEAWRAS NPQLVQLFAT RMLHAASMMI
CGKLMLDQAL LAAKKLAELG EDHFDAMFYK GKIATARFYV MNVVPGVFGT LKAMKVADTS
AIDMPEEAFM
