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Benzoyl-CoA reductase subunit D (EC 1.3.7.8) (3-hydroxybenzoyl-CoA reductase subunit delta) (EC 1.3.99.n1)

 BCRD_THAAR              Reviewed;         282 AA.
O87877;
23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
30-AUG-2017, entry version 51.
RecName: Full=Benzoyl-CoA reductase subunit D;
EC=1.3.7.8 {ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
AltName: Full=3-hydroxybenzoyl-CoA reductase subunit delta;
EC=1.3.99.n1 {ECO:0000269|PubMed:11208796, ECO:0000269|PubMed:8575453};
Name=bcrD;
Thauera aromatica.
Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
Zoogloeaceae; Thauera.
NCBI_TaxID=59405;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-14, AND
SUBUNIT.
STRAIN=DSM 6984 / K172;
PubMed=9746358; DOI=10.1046/j.1432-1327.1998.2560148.x;
Breese K., Boll M., Alt-Moerbe J., Schaegger H., Fuchs G.;
"Genes coding for the benzoyl-CoA pathway of anaerobic aromatic
metabolism in the bacterium Thauera aromatica.";
Eur. J. Biochem. 256:148-154(1998).
[2]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
STRAIN=DSM 6984 / K172;
PubMed=8575453; DOI=10.1111/j.1432-1033.1995.921_a.x;
Boll M., Fuchs G.;
"Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of
anaerobic aromatic metabolism. ATP dependence of the reaction,
purification and some properties of the enzyme from Thauera aromatica
strain K172.";
Eur. J. Biochem. 234:921-933(1995).
[3]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=DSM 6984 / K172;
PubMed=11208796; DOI=10.1128/JB.183.3.968-979.2001;
Laempe D., Jahn M., Breese K., Schaegger H., Fuchs G.;
"Anaerobic metabolism of 3-hydroxybenzoate by the denitrifying
bacterium Thauera aromatica.";
J. Bacteriol. 183:968-979(2001).
-!- FUNCTION: Catalyzes the anaerobic reduction of benzoyl-CoA and 3-
hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and
3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The
enzyme also reduces other benzoyl-CoA analogs with small
substituents at the aromatic ring. {ECO:0000269|PubMed:8575453}.
-!- CATALYTIC ACTIVITY: Cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized
ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced
ferredoxin + 2 ATP + 2 H(2)O. {ECO:0000269|PubMed:11208796,
ECO:0000269|PubMed:8575453}.
-!- CATALYTIC ACTIVITY: 3-hydroxybenzoyl-CoA + reduced acceptor + 2
ATP + 2 H(2)O = 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA +
acceptor + 2 ADP + 2 phosphate. {ECO:0000269|PubMed:11208796,
ECO:0000269|PubMed:8575453}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000269|PubMed:8575453};
Note=The iron-sulfur cluster may be a [4Fe-4S] cluster.
{ECO:0000269|PubMed:8575453};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=15 uM for benzoyl-CoA {ECO:0000269|PubMed:11208796,
ECO:0000269|PubMed:8575453};
KM=20 uM for 3-hydroxybenzoyl-CoA {ECO:0000269|PubMed:11208796,
ECO:0000269|PubMed:8575453};
KM=600 uM for ATP {ECO:0000269|PubMed:11208796,
ECO:0000269|PubMed:8575453};
pH dependence:
Optimum pH is 7.2-7.5. {ECO:0000269|PubMed:11208796,
ECO:0000269|PubMed:8575453};
-!- SUBUNIT: Heterotetramer composed of A, B, C, and D subunits.
{ECO:0000269|PubMed:9746358}.
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EMBL; AJ224959; CAA12250.1; -; Genomic_DNA.
ProteinModelPortal; O87877; -.
SMR; O87877; -.
KEGG; ag:CAA12250; -.
KO; K04115; -.
BioCyc; MetaCyc:BCRDTHAUERA-MONOMER; -.
SABIO-RK; O87877; -.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0018522; F:benzoyl-CoA reductase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
InterPro; IPR002731; ATPase_BadF.
InterPro; IPR011956; Benzoyl_CoA_Rdtase_D.
InterPro; IPR008275; CoA_E_activase.
Pfam; PF01869; BcrAD_BadFG; 1.
TIGRFAMs; TIGR02261; benz_CoA_red_D; 1.
TIGRFAMs; TIGR00241; CoA_E_activ; 1.
1: Evidence at protein level;
4Fe-4S; Aromatic hydrocarbons catabolism; ATP-binding;
Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
Nucleotide-binding; Oxidoreductase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9746358}.
CHAIN 2 282 Benzoyl-CoA reductase subunit D.
/FTId=PRO_0000350733.
METAL 130 130 Iron-sulfur (4Fe-4S); shared with BcrA.
{ECO:0000255}.
METAL 169 169 Iron-sulfur (4Fe-4S); shared with BcrA.
{ECO:0000255}.
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


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