BCD2_SYNWW
ID BCD2_SYNWW Reviewed; 610 AA.
AC Q0AVA8;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Butyryl-CoA dehydrogenase Swol_2052 {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_2052 {ECO:0000312|EMBL:ABI69346.1};
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: Expressed during syntrophic growth with butyrate (at protein
CC level) (PubMed:19648244, PubMed:23468890). Seems to be constitutively
CC expressed (PubMed:23468890). {ECO:0000269|PubMed:19648244,
CC ECO:0000269|PubMed:23468890}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CP000448; ABI69346.1; -; Genomic_DNA.
DR RefSeq; WP_011641438.1; NC_008346.1.
DR AlphaFoldDB; Q0AVA8; -.
DR SMR; Q0AVA8; -.
DR STRING; 335541.Swol_2052; -.
DR EnsemblBacteria; ABI69346; ABI69346; Swol_2052.
DR KEGG; swo:Swol_2052; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_12_2_9; -.
DR OMA; IEFARMM; -.
DR OrthoDB; 433393at2; -.
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:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
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 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_2052"
FT /id="PRO_0000442212"
FT ACT_SITE 451
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q06319"
SQ SEQUENCE 610 AA; 67931 MW; B2067E97A3A7197D CRC64;
MPHNNYLYQT RDIKFQIKEW LDINKILSLD AYKDYYGADD FDAICDVNFK ICRDVICPAN
KESDEIGMKH VGGNEKAVIS PDVFKTVYNT VIEAGMGPQF GDRQVEGRMP LYWYAPILEM
QTGASPAMVM LWCLTQGATT VLQYNLSKEL QERFLPKMYS GEWGGSMCLT EPGAGSEVGA
VSTKCFPTDT PGLWKVKGQK CFITTGDWDG VDNIIHLVLA KDPDAKPGTA GISCLVVPKF
WVNEDGSMGA WNDVTTTGIE HKLGIHGSAT CSLAFGENDN CYGWMIGDGP VDGRGQGMAQ
MFQMMNEERI NTGIFSLGAF GAAYYAALEY SKARVQSKKS TDPKGPSVRI IEHEDVRRML
LLQKSVMEAC RALLYSSYYY IDMSKEAATE EEREYAEDMF MIQNPLCKAY VSDMAWVMCA
EAIQVHGGYG FMEEYAPASL ARDCKIYTLW EGTNFIQSQD FTGRKFTMKK GEPFKKWLAE
IGDFIANKKT PEFAAEFAMM EKAFAAFNSI IDMNAAWTTT NKQLKQLFAT RIMHAAARVI
CGKLMLDQGL LAAGKLAELG DSHFDANFYK GKLASVKFYV MNVVPEIFGT EEAMKAADTS
AIDCPEEAIM
