O87876 (BCRA_THAAR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Benzoyl-CoA reductase subunit A
EC=1.3.7.8

Alternative name(s):
3-hydroxybenzoyl-CoA reductase subunit alpha
EC=1.3.99.n1

Gene names

Name:

bcrA

Organism

Thauera aromatica

Taxonomic identifier

59405 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Thauera

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
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. May be a 4Fe-4S cluster. 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	4Fe-4S ATP-binding 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	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity 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
	Chain	1 – 438	438	Benzoyl-CoA reductase subunit A		PRO_0000350730
Sites
	Metal binding	298	1	Iron-sulfur (4Fe-4S); shared with BcrD Potential
	Metal binding	337	1	Iron-sulfur (4Fe-4S); shared with BcrD Potential

Sequences

	Sequence		Length	Mass (Da)
	O87876 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 8F9E470FF688EAB7	FASTA	438	48,359
	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

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: 9746358] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17, SUBUNIT. Strain: DSM 6984 / K172.
[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: 8575453] [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: 11208796] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. Strain: DSM 6984 / K172.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ224959 Genomic DNA. Translation: CAA12249.1.
3D structure databases
HSSP	HSSP built from PDB template 1HUX based on UniProtKB P11568.
ProteinModelPortal	O87876.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:BCRATHAUERA-MONOMER.
BRENDA	1.3.99.15. 6271.
Family and domain databases
InterPro	IPR002731. ATPase_BadF. IPR011954. Benzoyl_CoA_Rdtase_A. IPR008275. CoA_E_activase. [Graphical view]
Pfam	PF01869. BcrAD_BadFG. 1 hit. [Graphical view]
TIGRFAMs	TIGR02259. Benz_CoA_red_A. 1 hit. TIGR00241. CoA_E_activ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BCRA_THAAR

Accession

Primary (citable) accession number: O87876

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	November 1, 1998
Last modified:	October 19, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program