BCRB_THAAR
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 03-AUG-2022, entry version 57.
DE RecName: Full=Benzoyl-CoA reductase subunit B;
DE EC=1.3.7.8 {ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
DE AltName: Full=3-hydroxybenzoyl-CoA reductase subunit beta;
DE EC=1.3.99.n1 {ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
GN Name=bcrB;
OS Thauera aromatica.
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=59405;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, AND SUBUNIT.
RX PubMed=9746358; 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 metabolism
RT in the bacterium Thauera aromatica.";
RL Eur. J. Biochem. 256:148-154(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND COFACTOR.
RC STRAIN=DSM 6984 / CIP 107765 / 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 anaerobic
RT aromatic metabolism. ATP dependence of the reaction, purification and some
RT properties of the enzyme from Thauera aromatica strain K172.";
RL Eur. J. Biochem. 234:921-933(1995).
RN [3]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DSM 6984 / CIP 107765 / K172;
RX 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 bacterium
RT 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 3-
CC hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme
CC also reduces other benzoyl-CoA analogs with small substituents at the
CC aromatic ring. {ECO:0000269|PubMed:8575453}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ADP + cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized 2[4Fe-
CC 4S]-[ferredoxin] + 2 phosphate = 2 ATP + benzoyl-CoA + 2 H2O +
CC reduced 2[4Fe-4S]-[ferredoxin]; Xref=Rhea:RHEA:30199, Rhea:RHEA-
CC COMP:10002, Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33722, ChEBI:CHEBI:33723,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57369, ChEBI:CHEBI:57374,
CC ChEBI:CHEBI:456216; EC=1.3.7.8;
CC Evidence={ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybenzoyl-CoA + AH2 + 2 ATP + 2 H2O = 3-
CC hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + A + 2 ADP + 2 H(+) + 2
CC phosphate; Xref=Rhea:RHEA:25420, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57342,
CC ChEBI:CHEBI:58801, ChEBI:CHEBI:456216; EC=1.3.99.n1;
CC Evidence={ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
CC -!- COFACTOR:
CC Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC Evidence={ECO:0000269|PubMed:8575453};
CC -!- COFACTOR:
CC Name=an oxidized flavin; Xref=ChEBI:CHEBI:60531;
CC Evidence={ECO:0000305|PubMed:8575453};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for benzoyl-CoA {ECO:0000269|PubMed:11208796,
CC ECO:0000269|PubMed:8575453};
CC KM=20 uM for 3-hydroxybenzoyl-CoA {ECO:0000269|PubMed:11208796,
CC ECO:0000269|PubMed:8575453};
CC KM=600 uM for ATP {ECO:0000269|PubMed:11208796,
CC ECO:0000269|PubMed:8575453};
CC pH dependence:
CC Optimum pH is 7.2-7.5. {ECO:0000269|PubMed:11208796,
CC ECO:0000269|PubMed:8575453};
CC -!- SUBUNIT: Heterotetramer composed of A, B, C, and D subunits.
CC {ECO:0000269|PubMed:9746358}.
CC -!- SIMILARITY: Belongs to the FldB/FldC dehydratase alpha/beta subunit
CC family. {ECO:0000305}.
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DR EMBL; AJ224959; CAA12248.1; -; Genomic_DNA.
DR AlphaFoldDB; O87875; -.
DR SMR; O87875; -.
DR KEGG; ag:CAA12248; -.
DR BioCyc; MetaCyc:BCRBTHAUERA-MON; -.
DR SABIO-RK; O87875; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0018522; F:benzoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR011955; Benzoyl_CoA_Rdtase_B.
DR InterPro; IPR010327; FldB/FldC_alpha/beta.
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; Direct protein sequencing;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; Nucleotide-binding;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9746358"
FT CHAIN 2..432
FT /note="Benzoyl-CoA reductase subunit B"
FT /id="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
