Reviewed, UniProtKB/Swiss-Prot O87877 (BCRD_THAAR)

Names and origin

Protein names

Recommended name:
    Benzoyl-CoA reductase subunit D
    EC=1.3.99.15
Alternative name(s):
    3-hydroxybenzoyl-CoA reductase subunit delta
    EC=1.3.99.n1

Gene names

Name:

bcrD

Organism

Thauera aromatica

Taxonomic identifier

59405 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Thauera

Protein attributes

Sequence length	282 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	Benzoyl-CoA + reduced acceptor + 2 ATP = cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + 2 ADP + 2 phosphate. Ref.2 Ref.3 3-hydroxybenzoyl-CoA + reduced acceptor + 2 ATP = 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 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 oxidation reduction 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 benzoyl-CoA reductase activity Inferred from electronic annotation. Source: EC iron 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 – 282	281	Benzoyl-CoA reductase subunit D		PRO_0000350733
Sites
	Metal binding	130	1	Iron-sulfur (4Fe-4S); shared with bcrA Potential
	Metal binding	169	1	Iron-sulfur (4Fe-4S); shared with bcrA Potential

Sequences

	Sequence		Length	Mass (Da)
	O87877-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 248D3D6305C90514	FASTA	282	30,157
	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

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 2-14, 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ224959 Genomic DNA. Translation: CAA12250.1.
3D structure databases
HSSP	HSSP built from PDB template 1HUX based on UniProtKB P11568.
ModBase	Search...
Family and domain databases
InterPro	IPR002731. ATPase_BadF. IPR011956. Benzoyl_CoA_Rdtase_D. IPR008275. CoA_E_activase. [Graphical view]
Pfam	PF01869. BcrAD_BadFG. 1 hit. [Graphical view]
ProDom	PD006344. CoA_E_activase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR02261. benz_CoA_red_D. 1 hit. TIGR00241. CoA_E_activ. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BCRD_THAAR

Accession

Primary (citable) accession number: O87877

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)