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 08-MAY-2019, entry version 56. DE RecName: Full=Benzoyl-CoA reductase subunit A; DE EC=1.3.7.8 {ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453}; DE AltName: Full=3-hydroxybenzoyl-CoA reductase subunit alpha; DE EC=1.3.99.n1 {ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453}; GN Name=bcrA; OS Thauera aromatica. OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; OC Zoogloeaceae; 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 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 RT metabolism in the bacterium Thauera aromatica."; RL Eur. J. Biochem. 256:148-154(1998). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, RP BIOPHYSICOCHEMICAL 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 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. {ECO:0000269|PubMed:8575453}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 ADP + cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized CC 2[4Fe-4S]-[ferredoxin] + 2 phosphate = 2 ATP + benzoyl-CoA + 2 CC H2O + reduced 2[4Fe-4S]-[ferredoxin]; Xref=Rhea:RHEA:30199, CC Rhea:RHEA-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, CC 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(+) + CC 2 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, CC ECO:0000269|PubMed:8575453}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000269|PubMed:8575453}; CC Note=The iron-sulfur cluster may be a [4Fe-4S] cluster. CC {ECO:0000269|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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ224959; CAA12249.1; -; Genomic_DNA. DR SMR; O87876; -. DR KEGG; ag:CAA12249; -. DR KO; K04114; -. DR BioCyc; MetaCyc:BCRATHAUERA-MONOMER; -. DR BRENDA; 1.3.7.8; 6271. DR SABIO-RK; O87876; -. 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:0018522; F:benzoyl-CoA reductase activity; IEA:UniProtKB-EC. 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; 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 {ECO:0000255}. FT METAL 337 337 Iron-sulfur (4Fe-4S); shared with BcrD. FT {ECO:0000255}. 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 //