[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17, 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. May be a 4Fe-4S cluster.
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; CAA12249.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P11568; 1HUX. [HSSP ENTRY / PDB]

ModBase

O87876.

Ontologies

GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
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: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

IPR002731; ATPase_BadF.
IPR011954; Benz_CoA_red_A.
IPR008275; CoA_E_activase.
Graphical view of domain structure.

Pfam

PF01869; BcrAD_BadFG; 1.
Pfam graphical view of domain structure.

ProDom

PD006344; CoA_E_activase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR02259; benz_CoA_red_A; 1.
TIGR00241; CoA_E_activ; 1.

ProtoNet

O87876.

Other

UniRef

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

Keywords

4Fe-4S; Aromatic hydrocarbons catabolism; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 438`	`438`	`Benzoyl-CoA reductase subunit A.`	`PRO_0000350730`
`METAL`	`298 298`		`Iron-sulfur (4Fe-4S); shared with bcrD (Potential).`
`METAL`	`337 337`		`Iron-sulfur (4Fe-4S); shared with bcrD (Potential).`

Sequence information

Length: 438 AA [This is the length of the unprocessed precursor]

Molecular weight: 48359 Da [This is the MW of the unprocessed precursor]

CRC64: 8F9E470FF688EAB7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MECFVGIDLG STTTKAVVMD DKGQVLGRGI TNSRSNYDTA ARVSKLEAFI DARLSLIRRE 

        70         80         90        100        110        120 
LDKEPAVAGR VDEIIDGLTR NFRREQFIEQ LGDLEQTCVA NVEGPRFAGK EKAIVGALTE 

       130        140        150        160        170        180 
VFRRLREEEA DKLFAPDAQR KSDFFRDLAG SRFMQIGEEV ARANGVEFDH LLHMYDKSII 

       190        200        210        220        230        240 
EVENRPPSAD MNRKFRSAME RVRGEMSSAL DTAALGAPID AALEIDMSER YVVGTGYGRV 

       250        260        270        280        290        300 
RLPFPKEHIR SEILCHGLGA HLMYPKTRTV LDIGGQDTKG IQIDDKGIVV NFQMNDRCAA 

       310        320        330        340        350        360 
GTGRYLGYVA DEMNMGLHEL GPLAMKSTKS IRINSTCTVF AGAELRDRLA LGDKREDILA 

       370        380        390        400        410        420 
GLHRAIMLRA MSIISRSGGI TDQFTFTGGV AKNEAAVKEL RQLVKENYGE VQINIDPDSI 

       430 
YTGALGASEF ARRAVVEA

O87876 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