ID   BCRA_THAAR              Reviewed;         438 AA.
AC   O87876;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   19-OCT-2011, entry version 38.
DE   RecName: Full=Benzoyl-CoA reductase subunit A;
DE            EC=1.3.7.8;
DE   AltName: Full=3-hydroxybenzoyl-CoA reductase subunit alpha;
DE            EC=1.3.99.n1;
GN   Name=bcrA;
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 1-17, AND
RP   SUBUNIT.
RC   STRAIN=DSM 6984 / K172;
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: Cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized
CC       ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced
CC       ferredoxin + 2 ATP + 2 H(2)O.
CC   -!- CATALYTIC ACTIVITY: 3-hydroxybenzoyl-CoA + reduced acceptor + 2
CC       ATP + 2 H(2)O = 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA +
CC       acceptor + 2 ADP + 2 phosphate.
CC   -!- COFACTOR: Iron-sulfur. May be a 4Fe-4S cluster.
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; CAA12249.1; -; Genomic_DNA.
DR   HSSP; P11568; 1HUX.
DR   ProteinModelPortal; O87876; -.
DR   BioCyc; MetaCyc:BCRATHAUERA-MONOMER; -.
DR   BRENDA; 1.3.99.15; 6271.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002731; ATPase_BadF.
DR   InterPro; IPR011954; Benzoyl_CoA_Rdtase_A.
DR   InterPro; IPR008275; CoA_E_activase.
DR   Pfam; PF01869; BcrAD_BadFG; 1.
DR   TIGRFAMs; TIGR02259; Benz_CoA_red_A; 1.
DR   TIGRFAMs; TIGR00241; CoA_E_activ; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Aromatic hydrocarbons catabolism; ATP-binding;
KW   Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW   Nucleotide-binding; Oxidoreductase.
FT   CHAIN         1    438       Benzoyl-CoA reductase subunit A.
FT                                /FTId=PRO_0000350730.
FT   METAL       298    298       Iron-sulfur (4Fe-4S); shared with BcrD
FT                                (Potential).
FT   METAL       337    337       Iron-sulfur (4Fe-4S); shared with BcrD
FT                                (Potential).
SQ   SEQUENCE   438 AA;  48359 MW;  8F9E470FF688EAB7 CRC64;
     MECFVGIDLG STTTKAVVMD DKGQVLGRGI TNSRSNYDTA ARVSKLEAFI DARLSLIRRE
     LDKEPAVAGR VDEIIDGLTR NFRREQFIEQ LGDLEQTCVA NVEGPRFAGK EKAIVGALTE
     VFRRLREEEA DKLFAPDAQR KSDFFRDLAG SRFMQIGEEV ARANGVEFDH LLHMYDKSII
     EVENRPPSAD MNRKFRSAME RVRGEMSSAL DTAALGAPID AALEIDMSER YVVGTGYGRV
     RLPFPKEHIR SEILCHGLGA HLMYPKTRTV LDIGGQDTKG IQIDDKGIVV NFQMNDRCAA
     GTGRYLGYVA DEMNMGLHEL GPLAMKSTKS IRINSTCTVF AGAELRDRLA LGDKREDILA
     GLHRAIMLRA MSIISRSGGI TDQFTFTGGV AKNEAAVKEL RQLVKENYGE VQINIDPDSI
     YTGALGASEF ARRAVVEA
//