ID   BAMA_SYNAS              Reviewed;         382 AA.
AC   Q2LXU2;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase {ECO:0000303|PubMed:18312395};
DE            Short=6-OCH-CoA hydrolase {ECO:0000303|PubMed:18312395};
DE            EC=3.7.1.21 {ECO:0000269|PubMed:18312395};
DE   AltName: Full=6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase {ECO:0000305};
GN   Name=bamA {ECO:0000303|PubMed:18312395}; ORFNames=SYN_01654;
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, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=SB;
RX   PubMed=18312395; DOI=10.1111/j.1462-2920.2008.01570.x;
RA   Kuntze K., Shinoda Y., Moutakki H., McInerney M.J., Vogt C., Richnow H.H.,
RA   Boll M.;
RT   "6-Oxocyclohex-1-ene-1-carbonyl-coenzyme A hydrolases from obligately
RT   anaerobic bacteria: characterization and identification of its gene as a
RT   functional marker for aromatic compounds degrading anaerobes.";
RL   Environ. Microbiol. 10:1547-1556(2008).
CC   -!- FUNCTION: Involved in the central benzoyl-CoA catabolism. Catalyzes the
CC       addition of one molecule of water to the double bond and the hydrolytic
CC       cleavage of C-C bond in the alicyclic ring, 6-oxocyclohex-1-ene-1-
CC       carbonyl-CoA (6-OCH-CoA) to yield 3-hydroxypimelyl-CoA.
CC       {ECO:0000269|PubMed:18312395}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-oxocyclohex-1-ene-1-carbonyl-CoA + 2 H2O = 3-hydroxy-6-
CC         carboxyhexanoyl-CoA + H(+); Xref=Rhea:RHEA:39651, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57343, ChEBI:CHEBI:76526; EC=3.7.1.21;
CC         Evidence={ECO:0000269|PubMed:18312395};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=115 uM for 6-OCH-CoA {ECO:0000269|PubMed:18312395};
CC   -!- PATHWAY: Aromatic compound metabolism; benzoyl-CoA degradation.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:18312395}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000252; ABC78905.1; -; Genomic_DNA.
DR   RefSeq; WP_011418920.1; NC_007759.1.
DR   AlphaFoldDB; Q2LXU2; -.
DR   SMR; Q2LXU2; -.
DR   STRING; 56780.SYN_01654; -.
DR   EnsemblBacteria; ABC78905; ABC78905; SYN_01654.
DR   KEGG; sat:SYN_01654; -.
DR   eggNOG; COG1024; Bacteria.
DR   HOGENOM; CLU_729117_0_0_7; -.
DR   OMA; AILGCDK; -.
DR   OrthoDB; 1275789at2; -.
DR   BioCyc; MetaCyc:MON-18322; -.
DR   BRENDA; 3.7.1.21; 14300.
DR   UniPathway; UPA00739; -.
DR   Proteomes; UP000001933; Chromosome.
DR   GO; GO:0018807; F:6-hydroxycyclohex-1-ene-1-carboxyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IDA:UniProtKB.
DR   GO; GO:1901788; P:benzoyl-CoA catabolic process; IDA:UniProtKB.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR017613; Dearomat_hydrolase.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR03200; dearomat_oah; 1.
DR   PROSITE; PS50270; NGF_2; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..382
FT                   /note="6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase"
FT                   /id="PRO_0000430864"
SQ   SEQUENCE   382 AA;  43102 MW;  85516C57287BDFC1 CRC64;
     MSLDWMPREH GLKNHSRHTE QWWGTEAPCT VYEKRPLKDP KGNVVPGLYS AWIRLNNPGQ
     YNSYTTEMVK GVIAGFENSS TDREVVAVVF TGTGPNAFCT GGNTKEYSEY YSMRPEEYGS
     YMELFNNMVD SILMCKKPVI CRVNGMRVAG GQEIGTATDI TVSSDLAIFG QAGPRHGSAP
     VGGASDFLPW FLSIEDAMWN CVSCEMWSAY KMKAKNLISK ALPVLKDDKG NWVRNPQVYT
     DTYVKDGEIV YGEPKTGEEA KQARAWVNEK LKNNDYDFSL IDAEVDRIVW VFANLFPGCL
     MKSIDGIRQK KKFWWDQIKN DHRYWLGTNM MGEAFLGFGA FNTKKITGKD TIDFIKNRQL
     IAEGALVDEA FMEQVLGKPL AK