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O87875 (BCRB_THAAR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 34. 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 B

EC=1.3.7.8
Alternative name(s):
3-hydroxybenzoyl-CoA reductase subunit beta
EC=1.3.99.n1
Gene names
Name:bcrB
OrganismThauera aromatica
Taxonomic identifier59405 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeThauera

Protein attributes

Sequence length432 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. Ref.2

Flavin Probable. 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 – 432431Benzoyl-CoA reductase subunit B
PRO_0000350731

Sequences

Sequence LengthMass (Da)Tools
O87875 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: B51374073291E8DE

FASTA43248,803
        10         20         30         40         50         60 
MSAKTNPEVI KESSMVKQKE MIAGNYDRLT GTKESGEKVV STFVPGNLNE LIMCFDMVNN 

        70         80         90        100        110        120 
LPETNAIQNG MRKQSGGMIM DAEKAGHSED VCTYVKADIG MMGRGNIAPN GKPMPAPDML 

       130        140        150        160        170        180 
LLSYTGCFTF MKWFELLRHE YKCPTVMLQI PYQGDGKITK NMRDFVVKQL KEEVIPMFEQ 

       190        200        210        220        230        240 
VSGVKFDIDR LREYLKNSAK AEDDLVWVLE SAKNRPSPID AYFGGVYYIG PMFTAFRGTA 

       250        260        270        280        290        300 
DAVEYYGLLR GEIEQRIREG KGPITPEGDM KEEKYRLVVE GPPNWTSFRE FWKLFYDEGA 

       310        320        330        340        350        360 
VVVASSYTKV GGLYDQGFRH DPNDPLGTLA DYCLGCYTNN NLPQRVELLE KYMNEYQADG 

       370        380        390        400        410        420 
LLINSIKSCN SFSAGQLLMM REIEKRTGKP AAFIETDLVD PRYFSHANVK NRLESYFQMV 

       430 
DQKRSGASLA TA 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, SUBUNIT.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: DSM 6984 / K172.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ224959 Genomic DNA. Translation: CAA12248.1.

3D structure databases

ProteinModelPortalO87875.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:BCRBTHAUERA-MONOMER.
SABIO-RKO87875.

Family and domain databases

InterProIPR011955. Benzoyl_CoA_Rdtase_B.
IPR010327. HGD-D.
[Graphical view]
PfamPF06050. HGD-D. 1 hit.
[Graphical view]
TIGRFAMsTIGR02260. benz_CoA_red_B. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBCRB_THAAR
AccessionPrimary (citable) accession number: O87875
Entry history
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: November 1, 1998
Last modified: April 3, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program