ID BCRD_THAAR Reviewed; 282 AA. AC O87877; DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Benzoyl-CoA reductase subunit D; DE EC=1.3.99.15; DE AltName: Full=3-hydroxybenzoyl-CoA reductase subunit delta; DE EC=1.3.99.n1; GN Name=bcrD; 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 2-14, 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: 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. 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ224959; CAA12250.1; -; Genomic_DNA. DR HSSP; P11568; 1HUX. 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:EC. DR GO; GO:0005506; F:iron ion 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; IPR002731; ATPase_BadF. DR InterPro; IPR011956; Benzoyl_CoA_Rdtase_D. DR InterPro; IPR008275; CoA_E_activase. DR Pfam; PF01869; BcrAD_BadFG; 1. DR ProDom; PD006344; CoA_E_activase; 1. DR TIGRFAMs; TIGR02261; benz_CoA_red_D; 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 INIT_MET 1 1 Removed. FT CHAIN 2 282 Benzoyl-CoA reductase subunit D. FT /FTId=PRO_0000350733. FT METAL 130 130 Iron-sulfur (4Fe-4S); shared with bcrA FT (Potential). FT METAL 169 169 Iron-sulfur (4Fe-4S); shared with bcrA FT (Potential). SQ SEQUENCE 282 AA; 30157 MW; 248D3D6305C90514 CRC64; MTITAGIDIG TGAVKTVLFR VEGDKTEWLA KRNDRIRQRD PFKLAEEAYN GLLEEAGLKA SDVDYVATTG EGESLAFHTG HFYSMTTHAR GAVYLNPEAR AVLDIGALHG RAIRNDERGK VETYKMTSQC ASGSGQFLEN IARYLGIAQD EIGSLSTQAD NPEVVSSICA VLAETDVINM VSRGISAPNI LKGIHISMAG RLAKLLKSVG ARDGVVLCTG GLALDEGLLK TLNESIQEQK MAVVAYNHPD SPYAGAIGAA LWGAFRHEKL ARLGQQQVAE AA //