BCRD_THAAR
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 03-AUG-2022, entry version 60.
DE RecName: Full=Benzoyl-CoA reductase subunit D;
DE EC=1.3.7.8 {ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
DE AltName: Full=3-hydroxybenzoyl-CoA reductase subunit delta;
DE EC=1.3.99.n1 {ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
GN Name=bcrD;
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 2-14, 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=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=[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}.
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DR EMBL; AJ224959; CAA12250.1; -; Genomic_DNA.
DR AlphaFoldDB; O87877; -.
DR SMR; O87877; -.
DR KEGG; ag:CAA12250; -.
DR BioCyc; MetaCyc:BCRDTHAUERA-MON; -.
DR SABIO-RK; O87877; -.
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; IPR043129; ATPase_NBD.
DR InterPro; IPR011956; Benzoyl_CoA_Rdtase_D.
DR InterPro; IPR008275; CoA_E_activase.
DR Pfam; PF01869; BcrAD_BadFG; 1.
DR SUPFAM; SSF53067; SSF53067; 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
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9746358"
FT CHAIN 2..282
FT /note="Benzoyl-CoA reductase subunit D"
FT /id="PRO_0000350733"
FT BINDING 130
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared with BcrA"
FT /evidence="ECO:0000255"
FT BINDING 169
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared with BcrA"
FT /evidence="ECO:0000255"
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
