[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, AND SUBUNIT. DOI=10.1046/j.1432-1327.1998.2560148.x; PubMed=9746358 [NCBI, ExPASy, EBI, Israel, Japan] 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]	CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR. STRAIN=DSM 6984 / K172; DOI=10.1111/j.1432-1033.1995.921_a.x; PubMed=8575453 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1128/JB.183.3.968-979.2001; PubMed=11208796 [NCBI, ExPASy, EBI, Israel, Japan] 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).

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: Benzoyl-CoA + reduced acceptor + 2 ATP = cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2 phosphate.
CATALYTIC ACTIVITY: 3-hydroxybenzoyl-CoA + reduced acceptor + 2 ATP = 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2 phosphate.
COFACTOR: Iron-sulfur.
COFACTOR: Flavin (Probable).
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=15 µM for benzoyl-CoA;
K_M=20 µM for 3-hydroxybenzoyl-CoA;
K_M=600 µM for ATP;
pH dependence: Optimum pH is 7.2-7.5;
SUBUNIT: Heterotetramer composed of A, B, C, and D subunits.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ224959; CAA12248.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

O87875.

Ontologies

GO:0018522;	Molecular function: benzoyl-CoA reductase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051536;	Molecular function: iron-sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR011955; Benz_CoA_red_B.
IPR010327; HGD-D.
Graphical view of domain structure.

Pfam

PF06050; HGD-D; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02260; benz_CoA_red_B; 1.

ProtoNet

O87875.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aromatic hydrocarbons catabolism; Direct protein sequencing; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 432`	`431`	`Benzoyl-CoA reductase subunit B.`	`PRO_0000350731`

Sequence information

Length: 432 AA [This is the length of the unprocessed precursor]

Molecular weight: 48803 Da [This is the MW of the unprocessed precursor]

CRC64: B51374073291E8DE [This is a checksum on the sequence]

        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

O87875 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools