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BOXC_AROEV
ID   BOXC_AROEV              Reviewed;         555 AA.
AC   Q84HH6;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Benzoyl-CoA-dihydrodiol lyase;
DE            EC=4.1.2.44 {ECO:0000269|PubMed:15916608, ECO:0000269|PubMed:20452977};
GN   Name=boxC;
OS   Aromatoleum evansii (Azoarcus evansii).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=59406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, AND INDUCTION.
RC   STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX   PubMed=12399500; DOI=10.1128/jb.184.22.6301-6315.2002;
RA   Gescher J., Zaar A., Mohamed M.E.-S., Schaegger H., Fuchs G.;
RT   "Genes coding for a new pathway of aerobic benzoate metabolism in Azoarcus
RT   evansii.";
RL   J. Bacteriol. 184:6301-6315(2002).
RN   [2]
RP   CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   CHARACTERIZATION, AND SUBUNIT.
RC   STRAIN=DSM 6898 / NBRC 107771 / KB740;
RX   PubMed=15916608; DOI=10.1111/j.1365-2958.2005.04637.x;
RA   Gescher J., Eisenreich W., Woerth J., Bacher A., Fuchs G.;
RT   "Aerobic benzoyl-CoA catabolic pathway in Azoarcus evansii: studies on the
RT   non-oxygenolytic ring cleavage enzyme.";
RL   Mol. Microbiol. 56:1586-1600(2005).
RN   [3]
RP   CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX   PubMed=20452977; DOI=10.1074/jbc.m110.124156;
RA   Rather L.J., Knapp B., Haehnel W., Fuchs G.;
RT   "Coenzyme A-dependent aerobic metabolism of benzoate via epoxide
RT   formation.";
RL   J. Biol. Chem. 285:20615-20624(2010).
CC   -!- FUNCTION: Catalyzes the ring opening of 2,3-epoxy-2,3-dihydroxybenzoyl-
CC       CoA to form 3,4-didehydroadipyl-CoA semialdehyde.
CC       {ECO:0000269|PubMed:15916608}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-epoxy-2,3-dihydrobenzoyl-CoA + 2 H2O = (3Z)-6-oxohex-3-
CC         enoyl-CoA + formate + H(+); Xref=Rhea:RHEA:48308, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:58787,
CC         ChEBI:CHEBI:88118; EC=4.1.2.44;
CC         Evidence={ECO:0000269|PubMed:15916608, ECO:0000269|PubMed:20452977};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=17 uM for 2,3-epoxy-2,3-dihydroxybenzoyl-CoA
CC         {ECO:0000269|PubMed:15916608};
CC         Vmax=4.9 umol/min/mg enzyme for the forward reaction
CC         {ECO:0000269|PubMed:15916608};
CC         Note=The substrate was earlier believed to be 2,3-dihydro-2,3-
CC         dihydroxybenzoyl-CoA but it has later been shown to be the epoxide as
CC         the substrate was enzymatically produced by BoxAB.
CC         {ECO:0000305|PubMed:20452977};
CC       pH dependence:
CC         Optimum pH is 9. {ECO:0000269|PubMed:15916608};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15916608}.
CC   -!- INDUCTION: By benzoate. {ECO:0000269|PubMed:12399500}.
CC   -!- SIMILARITY: Belongs to the benzoyl-CoA oxygenase component C family.
CC       {ECO:0000305}.
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DR   EMBL; AF548005; AAN39375.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q84HH6; -.
DR   SMR; Q84HH6; -.
DR   KEGG; ag:AAN39375; -.
DR   BioCyc; MetaCyc:MON-15412; -.
DR   BRENDA; 4.1.2.44; 603.
DR   SABIO-RK; Q84HH6; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR017633; Benz-CoA_dihydrodiol_lyase.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 2.
DR   TIGRFAMs; TIGR03222; benzo_boxC; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; Lyase.
FT   CHAIN           1..555
FT                   /note="Benzoyl-CoA-dihydrodiol lyase"
FT                   /id="PRO_0000350728"
SQ   SEQUENCE   555 AA;  61083 MW;  207F5ADAB26EC922 CRC64;
     MQAVANKPVA ELVDYRTEPS KYRHWSLATD GEIATLTLNI DEDGGIRPGY KLKLNSYDLG
     VDIELHDALQ RVRFEHPEVR TVVVTSGKPK IFCSGANIYM LGLSTHAWKV NFCKFTNETR
     NGIEDSSQYS GLKFLAACNG TTAGGGYELA LACDEIVLVD DRNSSVSLPE VPLLGVLPGT
     GGLTRVTDKR RVRRDHADIF CTISEGVRGQ RAKDWRLVDD VVKQQQFAEH IQARAKALAQ
     TSDRPAGAKG VKLTTLERTV DEKGYHYEFV DATIDADGRT VTLTVRAPAA VTAKTAAEIE
     AQGIKWWPLQ MARELDDAIL NLRTNHLDVG LWQLRTEGDA QVVLDIDATI DANRDNWFVR
     ETIGMLRRTL ARIDVSSRSL YALIEPGSCF AGTLLEIALA ADRSYMLDAA EAKNVVGLSA
     MNFGTFPMVN GLSRIDARFY QEEAPVAAVK AKQGSLLSPA EAMELGLVTA IPDDLDWAEE
     VRIAIEERAA LSPDALTGLE ANLRFGPVET MNTRIFGRLS AWQNWIFNRP NAVGENGALK
     LFGSGKKAQF DWNRV
 
 
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