ID   CHCOA_SYNAS             Reviewed;         384 AA.
AC   Q2LQP0;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cyclohexane-1-carbonyl-CoA dehydrogenase {ECO:0000305};
DE            Short=ChCoA {ECO:0000303|PubMed:23667239};
DE            EC=1.3.8.11 {ECO:0000269|PubMed:23667239};
GN   ORFNames=SYN_02586 {ECO:0000312|EMBL:ABC76100.1};
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   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP   COFACTOR, SUBUNIT, AND BIOPHYSICOCHEMICAL 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 cyclohexane-1-carbonyl-CoA into
CC       cyclohex-1-ene-1-carbonyl-CoA in biosynthesis of cyclohexane-1-
CC       carboxylate, a by-product produced during fermentation of benzoate and
CC       crotonate to acetate. {ECO:0000269|PubMed:23667239}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclohexane-1-carbonyl-CoA + H(+) + oxidized [electron-
CC         transfer flavoprotein] = cyclohex-1-ene-1-carbonyl-CoA + reduced
CC         [electron-transfer flavoprotein]; Xref=Rhea:RHEA:38935, Rhea:RHEA-
CC         COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:76270,
CC         ChEBI:CHEBI:76271; EC=1.3.8.11;
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=22 uM for cyclohexane-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; ABC76100.1; -; Genomic_DNA.
DR   RefSeq; WP_011416134.1; NC_007759.1.
DR   AlphaFoldDB; Q2LQP0; -.
DR   SMR; Q2LQP0; -.
DR   STRING; 56780.SYN_02586; -.
DR   EnsemblBacteria; ABC76100; ABC76100; SYN_02586.
DR   KEGG; sat:SYN_02586; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_7; -.
DR   OMA; YAIPQQW; -.
DR   OrthoDB; 760677at2; -.
DR   BioCyc; MetaCyc:MON-18318; -.
DR   SABIO-RK; Q2LQP0; -.
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..384
FT                   /note="Cyclohexane-1-carbonyl-CoA dehydrogenase"
FT                   /id="PRO_0000430698"
SQ   SEQUENCE   384 AA;  42063 MW;  B61BD8560E26FFD4 CRC64;
     MYINTETEDL KTAIDAIRKA VKDRIAPLAA EVDDSGVIKP EIYDLLWDLG LMTVTYPPEY
     GGSETNPGTL LCIGCEEIAK ACASTALLLI IQAVGSFPLM HGGRKELLDR IAPRIVNNRE
     LAGYLVSEPG AGSDVKAIRT KAVKDGNDWV INGTKCWATN GPIASFYSCL CRTKDDKGVQ
     GYSFFLVERN TPGLSVGKIE HKMGMRGSQT SEVILEDVRV PAENLLGELN NGFKLAMKDF
     DMSRPAIAAQ ALGISEGAFA QMETYSRERY TFGKPLCEHG MITQIIADSA ALIEAGRGLI
     YQAADLYDKG KKNTKLASMA KFFMGDAAVK ITTDAIQVFG GYGYTHDYPV ERMFRDAKLT
     QIFEGANQIQ RIVVAREIRD EQSK