ID   BAMA_GEOMG              Reviewed;         381 AA.
AC   Q39TV7;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
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:16313613}; OrderedLocusNames=Gmet_2088;
OS   Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INDUCTION.
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RX   PubMed=16313613; DOI=10.1111/j.1365-2958.2005.04909.x;
RA   Wischgoll S., Heintz D., Peters F., Erxleben A., Sarnighausen E., Reski R.,
RA   Van Dorsselaer A., Boll M.;
RT   "Gene clusters involved in anaerobic benzoate degradation of Geobacter
RT   metallireducens.";
RL   Mol. Microbiol. 58:1238-1252(2005).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15;
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=70 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   -!- INDUCTION: By benzoate. {ECO:0000269|PubMed:16313613}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000148; ABB32317.1; -; Genomic_DNA.
DR   RefSeq; WP_004514578.1; NC_007517.1.
DR   AlphaFoldDB; Q39TV7; -.
DR   SMR; Q39TV7; -.
DR   STRING; 269799.Gmet_2088; -.
DR   EnsemblBacteria; ABB32317; ABB32317; Gmet_2088.
DR   KEGG; gme:Gmet_2088; -.
DR   eggNOG; COG1024; Bacteria.
DR   HOGENOM; CLU_729117_0_0_7; -.
DR   OMA; AILGCDK; -.
DR   OrthoDB; 1275789at2; -.
DR   UniPathway; UPA00739; -.
DR   Proteomes; UP000007073; 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; IPR018376; Enoyl-CoA_hyd/isom_CS.
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; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..381
FT                   /note="6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase"
FT                   /id="PRO_0000430863"
SQ   SEQUENCE   381 AA;  41952 MW;  0ACE5FECC5F587BB CRC64;
     MARTDEIIAR TAPGHLNDHN LIDREVESLC DGMVKYEKRP AKRHDGSVAE GIYNAWIILD
     NPKQYNSYTT DMVKAIILAF RRASVDRSVN AVVFTGVGDK AFCTGGNTKE YAEYYAGNPQ
     EYRQYMRLFN DMVSAILGCD KAVISRVNGM RIGGGQEIGM ACDFSIAQDL ANFGQAGPKH
     GSAAIGGATD FLPLMVGCEQ AMVSGTLCEP FSAHKAARLG IICDVVPALK VGGKFVANPT
     VVTDRYLDEY GRVVHGEFKA GAAFKEGQGQ IKEGEIDLSL LDEKVESLCT KLLETFPECM
     TKSLEELRKP KLHAWNLNKE NSRAWLALNM MNEARTGFRA FNEGTKETGR EIDFVKLRQG
     LAKGTPWTEE LIESLMPTAQ K