ID   BCRB_THAAR              Reviewed;         432 AA.
AC   O87875;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Benzoyl-CoA reductase subunit B;
DE            EC=1.3.99.15;
DE   AltName: Full=3-hydroxybenzoyl-CoA reductase subunit beta;
DE            EC=1.3.99.n1;
GN   Name=bcrB;
OS   Thauera aromatica.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Thauera.
OX   NCBI_TaxID=59405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, AND
RP   SUBUNIT.
RX   MEDLINE=98417440; PubMed=9746358;
RX   DOI=10.1046/j.1432-1327.1998.2560148.x;
RA   Breese K., Boll M., Alt-Moerbe J., Schaegger H., Fuchs G.;
RT   "Genes coding for the benzoyl-CoA pathway of anaerobic aromatic
RT   metabolism in the bacterium Thauera aromatica.";
RL   Eur. J. Biochem. 256:148-154(1998).
RN   [2]
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND COFACTOR.
RC   STRAIN=DSM 6984 / K172;
RX   PubMed=8575453; DOI=10.1111/j.1432-1033.1995.921_a.x;
RA   Boll M., Fuchs G.;
RT   "Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of
RT   anaerobic aromatic metabolism. ATP dependence of the reaction,
RT   purification and some properties of the enzyme from Thauera aromatica
RT   strain K172.";
RL   Eur. J. Biochem. 234:921-933(1995).
RN   [3]
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=DSM 6984 / K172;
RX   MEDLINE=21142524; PubMed=11208796; DOI=10.1128/JB.183.3.968-979.2001;
RA   Laempe D., Jahn M., Breese K., Schaegger H., Fuchs G.;
RT   "Anaerobic metabolism of 3-hydroxybenzoate by the denitrifying
RT   bacterium Thauera aromatica.";
RL   J. Bacteriol. 183:968-979(2001).
CC   -!- FUNCTION: Catalyzes the anaerobic reduction of benzoyl-CoA and 3-
CC       hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and
CC       3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The
CC       enzyme also reduces other benzoyl-CoA analogs with small
CC       substituents at the aromatic ring.
CC   -!- CATALYTIC ACTIVITY: Benzoyl-CoA + reduced acceptor + 2 ATP =
CC       cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2
CC       phosphate.
CC   -!- CATALYTIC ACTIVITY: 3-hydroxybenzoyl-CoA + reduced acceptor + 2
CC       ATP = 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2
CC       ADP + 2 phosphate.
CC   -!- COFACTOR: Iron-sulfur.
CC   -!- COFACTOR: Flavin (Probable).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=15 uM for benzoyl-CoA;
CC         KM=20 uM for 3-hydroxybenzoyl-CoA;
CC         KM=600 uM for ATP;
CC       pH dependence:
CC         Optimum pH is 7.2-7.5;
CC   -!- SUBUNIT: Heterotetramer composed of A, B, C, and D subunits.
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DR   EMBL; AJ224959; CAA12248.1; -; Genomic_DNA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0018522; F:benzoyl-CoA reductase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR011955; Benzoyl_CoA_Rdtase_B.
DR   InterPro; IPR010327; HGD-D.
DR   Pfam; PF06050; HGD-D; 1.
DR   TIGRFAMs; TIGR02260; benz_CoA_red_B; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; ATP-binding;
KW   Direct protein sequencing; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; Nucleotide-binding; Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    432       Benzoyl-CoA reductase subunit B.
FT                                /FTId=PRO_0000350731.
SQ   SEQUENCE   432 AA;  48803 MW;  B51374073291E8DE CRC64;
     MSAKTNPEVI KESSMVKQKE MIAGNYDRLT GTKESGEKVV STFVPGNLNE LIMCFDMVNN
     LPETNAIQNG MRKQSGGMIM DAEKAGHSED VCTYVKADIG MMGRGNIAPN GKPMPAPDML
     LLSYTGCFTF MKWFELLRHE YKCPTVMLQI PYQGDGKITK NMRDFVVKQL KEEVIPMFEQ
     VSGVKFDIDR LREYLKNSAK AEDDLVWVLE SAKNRPSPID AYFGGVYYIG PMFTAFRGTA
     DAVEYYGLLR GEIEQRIREG KGPITPEGDM KEEKYRLVVE GPPNWTSFRE FWKLFYDEGA
     VVVASSYTKV GGLYDQGFRH DPNDPLGTLA DYCLGCYTNN NLPQRVELLE KYMNEYQADG
     LLINSIKSCN SFSAGQLLMM REIEKRTGKP AAFIETDLVD PRYFSHANVK NRLESYFQMV
     DQKRSGASLA TA
//