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O87877 (BCRD_THAAR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Benzoyl-CoA reductase subunit D
EC=1.3.7.8
Alternative name(s):
3-hydroxybenzoyl-CoA reductase subunit delta
EC=1.3.99.n1
Gene names
Name:bcrD
OrganismThauera aromatica
Taxonomic identifier59405 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Thauera

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

Cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O. Ref.2 Ref.3

3-hydroxybenzoyl-CoA + reduced acceptor + 2 ATP + 2 H2O = 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2 phosphate. Ref.2 Ref.3

Cofactor

Iron-sulfur. May be a 4Fe-4S cluster. Ref.2

Subunit structure

Heterotetramer composed of A, B, C, and D subunits. Ref.1

Biophysicochemical properties

Kinetic parameters:

KM=15 µM for benzoyl-CoA Ref.2 Ref.3

KM=20 µM for 3-hydroxybenzoyl-CoA

KM=600 µM for ATP

pH dependence:

Optimum pH is 7.2-7.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 282281Benzoyl-CoA reductase subunit D
PRO_0000350733

Sites

Metal binding1301Iron-sulfur (4Fe-4S); shared with BcrA Potential
Metal binding1691Iron-sulfur (4Fe-4S); shared with BcrA Potential

Sequences

Sequence LengthMass (Da)Tools
O87877 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 248D3D6305C90514

FASTA28230,157
        10         20         30         40         50         60 
MTITAGIDIG TGAVKTVLFR VEGDKTEWLA KRNDRIRQRD PFKLAEEAYN GLLEEAGLKA 

        70         80         90        100        110        120 
SDVDYVATTG EGESLAFHTG HFYSMTTHAR GAVYLNPEAR AVLDIGALHG RAIRNDERGK 

       130        140        150        160        170        180 
VETYKMTSQC ASGSGQFLEN IARYLGIAQD EIGSLSTQAD NPEVVSSICA VLAETDVINM 

       190        200        210        220        230        240 
VSRGISAPNI LKGIHISMAG RLAKLLKSVG ARDGVVLCTG GLALDEGLLK TLNESIQEQK 

       250        260        270        280 
MAVVAYNHPD SPYAGAIGAA LWGAFRHEKL ARLGQQQVAE AA

« Hide

References

[1]"Genes coding for the benzoyl-CoA pathway of anaerobic aromatic metabolism in the bacterium Thauera aromatica."
Breese K., Boll M., Alt-Moerbe J., Schaegger H., Fuchs G.
Eur. J. Biochem. 256:148-154(1998) [PubMed: 9746358] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-14, SUBUNIT.
Strain: DSM 6984 / K172.
[2]"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."
Boll M., Fuchs G.
Eur. J. Biochem. 234:921-933(1995) [PubMed: 8575453] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
Strain: DSM 6984 / K172.
[3]"Anaerobic metabolism of 3-hydroxybenzoate by the denitrifying bacterium Thauera aromatica."
Laempe D., Jahn M., Breese K., Schaegger H., Fuchs G.
J. Bacteriol. 183:968-979(2001) [PubMed: 11208796] [Abstract]
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: DSM 6984 / K172.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ224959 Genomic DNA. Translation: CAA12250.1.

3D structure databases

HSSPHSSP built from PDB template 1HUX based on UniProtKB P11568.
ProteinModelPortalO87877.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:BCRDTHAUERA-MONOMER.

Family and domain databases

InterProIPR002731. ATPase_BadF.
IPR011956. Benzoyl_CoA_Rdtase_D.
IPR008275. CoA_E_activase.
[Graphical view]
PfamPF01869. BcrAD_BadFG. 1 hit.
[Graphical view]
TIGRFAMsTIGR02261. Benz_CoA_red_D. 1 hit.
TIGR00241. CoA_E_activ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBCRD_THAAR
AccessionPrimary (citable) accession number: O87877
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: November 1, 1998
Last modified: October 19, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
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