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 27-NOV-2024, entry version 70. 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; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae; OC Thauera. OX NCBI_TaxID=59405; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17, AND SUBUNIT. RC STRAIN=DSM 6984 / CIP 107765 / 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 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=cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized 2[4Fe-4S]- CC [ferredoxin] + 2 ADP + 2 phosphate = reduced 2[4Fe-4S]-[ferredoxin] + CC benzoyl-CoA + 2 ATP + 2 H2O; 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 phosphate + CC 2 H(+); Xref=Rhea:RHEA:25420, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57342, ChEBI:CHEBI:58801, CC ChEBI:CHEBI:456216; EC=1.3.99.n1; CC Evidence={ECO:0000269|PubMed:11208796, 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 AlphaFoldDB; O87876; -. DR SMR; O87876; -. DR KEGG; ag:CAA12249; -. 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:0009056; P:catabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.30.420.40; -; 2. DR InterPro; IPR002731; ATPase_BadF. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR011954; Benzoyl_CoA_Rdtase_A. DR InterPro; IPR008275; CoA_E_activase_dom. DR InterPro; IPR051805; Dehydratase_Activator_Redct. DR NCBIfam; TIGR02259; benz_CoA_red_A; 1. DR NCBIfam; TIGR00241; CoA_E_activ; 1. DR PANTHER; PTHR32329; BIFUNCTIONAL PROTEIN [INCLUDES 2-HYDROXYACYL-COA DEHYDRATASE (N-TER) AND ITS ACTIVATOR DOMAIN (C_TERM)-RELATED; 1. DR PANTHER; PTHR32329:SF2; BIFUNCTIONAL PROTEIN [INCLUDES 2-HYDROXYACYL-COA DEHYDRATASE (N-TER) AND ITS ACTIVATOR DOMAIN (C_TERM)-RELATED; 1. DR Pfam; PF01869; BcrAD_BadFG; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 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 FT /note="Benzoyl-CoA reductase subunit A" FT /id="PRO_0000350730" FT BINDING 298 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with BcrD" FT /evidence="ECO:0000255" FT BINDING 337 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared with BcrD" FT /evidence="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 //