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UniProtKB/Swiss-Prot entry O87877


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BCRD_THAAR
Primary accession number O87877
Secondary accession numbers None
Integrated into Swiss-Prot on September 23, 2008
Sequence was last modified on November 1, 1998 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 22)
Name and origin of the protein
Protein name Benzoyl-CoA reductase subunit D
Synonyms EC 1.3.99.15
3-hydroxybenzoyl-CoA reductase subunit delta
EC 1.3.99.n1
Gene name
Name: bcrD
From
Thauera aromatica [TaxID: 59405] 
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Rhodocyclaceae; Thauera.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-14, 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:   KM=15 µM for benzoyl-CoA;
    KM=20 µM for 3-hydroxybenzoyl-CoA;
    KM=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; CAA12250.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P11568; 1HUX. [HSSP ENTRY / PDB]
ModBase O87877.
Ontologies
GO
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.
IPR011956; Benz_CoA_red_D.
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 TIGR02261; benz_CoA_red_D; 1.
TIGR00241; CoA_E_activ; 1.
ProtoNet O87877.
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
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   282  281     Benzoyl-CoA reductase subunit D. PRO_0000350733
METAL   130   130        Iron-sulfur (4Fe-4S); shared with bcrA (Potential). 
METAL   169   169        Iron-sulfur (4Fe-4S); shared with bcrA (Potential). 
Sequence information
Length: 282 AA [This is the length of the unprocessed precursor] Molecular weight: 30157 Da [This is the MW of the unprocessed precursor] CRC64: 248D3D6305C90514 [This is a checksum on the sequence]
        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 

O87877 in FASTA format

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