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