ID   CH1CO_SYNAS             Reviewed;         414 AA.
AC   Q2LQN9;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase {ECO:0000305};
DE            Short=Ch1CoA {ECO:0000303|PubMed:23667239};
DE            EC=1.3.8.10 {ECO:0000269|PubMed:23667239};
GN   ORFNames=SYN_02587 {ECO:0000312|EMBL:ABC76101.1};
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB;
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=23667239; DOI=10.1128/jb.00322-13;
RA   Kung J.W., Seifert J., von Bergen M., Boll M.;
RT   "Cyclohexanecarboxyl-coenzyme A (CoA) and cyclohex-1-ene-1-carboxyl-CoA
RT   dehydrogenases, two enzymes involved in the fermentation of benzoate and
RT   crotonate in Syntrophus aciditrophicus.";
RL   J. Bacteriol. 195:3193-3200(2013).
CC   -!- FUNCTION: Mediates the conversion of cyclohex-1-ene-1-carbonyl-CoA into
CC       (E)-2-cyclohex-1,5-diene-1-carbonyl-CoA in biosynthesis of cyclohexane-
CC       1-carboxylate, a by-product produced during fermentation of benzoate
CC       and crotonate to acetate. Also able to further convert (E)-2-cyclohex-
CC       1,5-diene-1-carbonyl-CoA to benzoyl-CoA. {ECO:0000269|PubMed:23667239}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclohex-1-ene-1-carbonyl-CoA + H(+) + oxidized [electron-
CC         transfer flavoprotein] = cyclohexa-1,5-diene-1-carbonyl-CoA + reduced
CC         [electron-transfer flavoprotein]; Xref=Rhea:RHEA:12993, Rhea:RHEA-
CC         COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57374, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:76270; EC=1.3.8.10;
CC         Evidence={ECO:0000269|PubMed:23667239};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:23667239};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=19 uM for (E)-2-cyclohex-1,5-diene-1-carbonyl-CoA
CC         {ECO:0000269|PubMed:23667239};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23667239}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000252; ABC76101.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2LQN9; -.
DR   SMR; Q2LQN9; -.
DR   STRING; 56780.SYN_02587; -.
DR   EnsemblBacteria; ABC76101; ABC76101; SYN_02587.
DR   KEGG; sat:SYN_02587; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_7; -.
DR   OMA; NMATWML; -.
DR   BioCyc; MetaCyc:MON-18319; -.
DR   SABIO-RK; Q2LQN9; -.
DR   Proteomes; UP000001933; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR   GO; GO:0052890; F:oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor; IDA:UniProtKB.
DR   GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
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; PS00073; ACYL_COA_DH_2; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..414
FT                   /note="Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase"
FT                   /id="PRO_0000430699"
SQ   SEQUENCE   414 AA;  45178 MW;  A3CA2502DEEAD4D8 CRC64;
     MKGPIKFNAL SLQGRSVMSN QSNDTTITQR RDTMNELTEE QKLLMEMVRN LAVREIAPRA
     IEIDENHSFP VHARDLFADL GLLSPLVPVE YGGTGMDITT FAMVLEEIGK VCASTALMLL
     AQADGMLSII LDGSPALKEK YLPRFGEKST LMTAFAATEP GAGSDLLAMK TRAVKKGDKY
     VINGQKCFIT NGSVADILTV WAYTDPSKGA KGMSTFVVER GTPGLIYGHN EKKMGMRGCP
     NSELFFEDLE VPAENLVGEE GKGFAYLMGA LSINRVFCAS QAVGIAQGAL ERAMQHTRER
     EQFGKPIAHL TPIQFMIADM ATEVEAARLL VRKATTLLDA KDKRGPLIGG MAKTFASDTA
     MKVTTDAVQV MGGSGYMQEY QVERMMREAK LTQIYTGTNQ ITRMVTGRSL LFPS