Reviewed, UniProtKB/Swiss-Prot O87874 (BCRC_THAAR)

Names and origin

Protein names

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

Gene names

Name:

bcrC

Organism

Thauera aromatica

Taxonomic identifier

59405 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Thauera

Protein attributes

Sequence length	386 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. Ref.2 Flavin Probable.
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	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 oxidation reduction 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 ion binding Inferred from electronic annotation. Source: UniProtKB-KW iron-sulfur cluster 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 – 386	385	Benzoyl-CoA reductase subunit C		PRO_0000350732

Sequences

	Sequence		Length	Mass (Da)
	O87874-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 989BC3528A45EC6E	FASTA	386	43,720
	10 20 30 40 50 60 MSTADIIARC EALYEDLDFT AARQWKEADP SRKVIAYMPV YVPREIIHAA GMLPLGIMGG 70 80 90 100 110 120 GDGLEVIHGD AFYQSYICRI PRSTIELGLS KRMDFVDGML FPSICDVIRN LSGMWKLMFP 130 140 150 160 170 180 GKYVRYFDVP QNYRDDVGGN YYTAELNELR EGLEHLSGRK ITDDALRASI KVYNENRKLV 190 200 210 220 230 240 QDVYGLRSRE PWKVPSADVY LLMRAGLVLP VEEHNQMLKD YLAAAVKVEA QKRDNCRVII 250 260 270 280 290 300 NGSFCEQPPL NLIKSIELSG CYIVDDDYMI VHRFLRNEVS TAGDPMQNLS LAFLHESIST 310 320 330 340 350 360 AAKYDDKEED KGKYLLEQVR TNAAEGVIFA APSFCDPALL ERPMLADRCS ENKVPYISFK 370 380 YAENSGQMQP IREQAGTFAD SIKLWS

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 2-18; 119-130 AND 218-229, 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: CAA12247.1.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR011958. Benzoyl_CoA_Rdtase_C. IPR010327. HGD-D. [Graphical view]
Pfam	PF06050. HGD-D. 1 hit. [Graphical view]
TIGRFAMs	TIGR02263. benz_CoA_red_C. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BCRC_THAAR

Accession

Primary (citable) accession number: O87874

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 23, 2008
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 22 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)