[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18; 119-130 AND 218-229, AND SUBUNIT. STRAIN=DSM 6984 / K172; 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; CAA12247.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

O87874.

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

IPR011958; Benz_CoA_red_C.
IPR010327; HGD-D.
Graphical view of domain structure.

Pfam

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

TIGRFAMs

TIGR02263; benz_CoA_red_C; 1.

ProtoNet

O87874.

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`	`2 386`	`385`	`Benzoyl-CoA reductase subunit C.`	`PRO_0000350732`

Sequence information

Length: 386 AA [This is the length of the unprocessed precursor]

Molecular weight: 43720 Da [This is the MW of the unprocessed precursor]

CRC64: 989BC3528A45EC6E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTADIIARC EALYEDLDFT AARQWKEADP SRKVIAYMPV YVPREIIHAA GMLPLGIMGG 

        70         80         90        100        110        120 
GDGLEVIHGD AFYQSYICRI PRSTIELGLS KRMDFVDGML FPSICDVIRN LSGMWKLMFP 

       130        140        150        160        170        180 
GKYVRYFDVP QNYRDDVGGN YYTAELNELR EGLEHLSGRK ITDDALRASI KVYNENRKLV 

       190        200        210        220        230        240 
QDVYGLRSRE PWKVPSADVY LLMRAGLVLP VEEHNQMLKD YLAAAVKVEA QKRDNCRVII 

       250        260        270        280        290        300 
NGSFCEQPPL NLIKSIELSG CYIVDDDYMI VHRFLRNEVS TAGDPMQNLS LAFLHESIST 

       310        320        330        340        350        360 
AAKYDDKEED KGKYLLEQVR TNAAEGVIFA APSFCDPALL ERPMLADRCS ENKVPYISFK 

       370        380 
YAENSGQMQP IREQAGTFAD SIKLWS

O87874 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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