O87875 (BCRB_THAAR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Thauera aromatica

Taxonomic identifier

59405 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Thauera

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	ATP-binding Flavoprotein Iron Iron-sulfur Metal-binding Nucleotide-binding
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW benzoyl-CoA reductase activity Inferred from electronic annotation. Source: EC iron-sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 432	431	Benzoyl-CoA reductase subunit B		PRO_0000350731

Sequences

	Sequence		Length	Mass (Da)
	O87875 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: B51374073291E8DE	FASTA	432	48,803
	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

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
ProteinModelPortal	O87875.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:BCRBTHAUERA-MONOMER.
SABIO-RK	O87875.
Family and domain databases
InterPro	IPR011955. Benzoyl_CoA_Rdtase_B. IPR010327. HGD-D. [Graphical view]
Pfam	PF06050. HGD-D. 1 hit. [Graphical view]
TIGRFAMs	TIGR02260. benz_CoA_red_B. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BCRB_THAAR

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program