Reviewed, UniProtKB/Swiss-Prot O33820 (HCRB_THAAR)

Names and origin

Protein names

Recommended name:
    4-hydroxybenzoyl-CoA reductase subunit beta
    EC=1.3.99.20

Gene names

Name:

hcrB

Organism

Thauera aromatica

Taxonomic identifier

59405 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Thauera

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes reductive dehydroxylation of 4-hydroxybenzoyl-CoA. Reaction is not reversible.
Catalytic activity	Benzoyl-CoA + acceptor = 4-hydroxybenzoyl-CoA + reduced acceptor.
Cofactor	FAD. Iron-sulfur. Molybdenum.
Enzyme regulation	Inactivated by low concentrations of cyanide.
Subunit structure	Heterohexamer of two alpha, two beta and two gamma subunits.
Sequence similarities	Contains 1 FAD-binding PCMH-type domain. To xanthine oxidases.

Ontologies

Keywords
Ligand	FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4-hydroxybenzoyl-CoA reductase activity Inferred from electronic annotation. Source: EC FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW iron-sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum 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

Chain

1 – 324

324

4-hydroxybenzoyl-CoA reductase subunit beta

PRO_0000083926

Regions

Domain

2 – 217

216

FAD-binding PCMH-type

Sites

Metal binding

117

1

Iron-sulfur Potential

Metal binding

122

1

Iron-sulfur Potential

Metal binding

138

1

Iron-sulfur Potential

Metal binding

146

1

Iron-sulfur Potential

Metal binding

155

1

Iron-sulfur Potential

Experimental info

Sequence conflict

22 – 30

9

LAAEATLPL → GTVPVAQLF AA sequence Ref.1

Secondary structure

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324

Helix Strand Turn

Details...

Beta strand

8 – 10

3

Helix

15 – 21

7

Beta strand

27 – 32

6

Helix

36 – 41

6

Beta strand

48 – 52

5

Turn

57 – 60

4

Beta strand

62 – 64

3

Beta strand

70 – 73

4

Helix

78 – 83

6

Helix

85 – 90

6

Helix

92 – 100

9

Helix

104 – 109

6

Helix

112 – 116

5

Turn

123 – 125

3

Helix

129 – 134

6

Beta strand

147 – 149

3

Helix

163 – 169

7

Beta strand

173 – 178

6

Beta strand

181 – 186

6

Helix

187 – 190

4

Beta strand

206 – 212

7

Beta strand

219 – 225

7

Beta strand

227 – 231

5

Beta strand

235 – 245

11

Beta strand

248 – 262

15

Helix

269 – 271

3

Helix

278 – 291

14

Beta strand

298 – 300

3

Helix

302 – 322

21

Sequences

	Sequence		Length	Mass (Da)
	O33820-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: C3C5ECAAD093F9DB	FASTA	324	34,374
	10 20 30 40 50 60 MNILTDFRTH RPATLADAVN ALAAEATLPL GAGTDLLPNL RRGLGHPAAL VDLTGIDGLA 70 80 90 100 110 120 TISTLADGSL RIGAGATLEA IAEHDAIRTT WPALAQAAES VAGPTHRAAA TLGGNLCQDT 130 140 150 160 170 180 RCTFYNQSEW WRSGNGYCLK YKGDKCHVIV KSDRCYATYH GDVAPALMVL DARAEIVGPA 190 200 210 220 230 240 GKRTVPVAQL FRESGAEHLT LEKGELLAAI EVPPTGAWSA AYSKVRIRDA VDFPLAGVAA 250 260 270 280 290 300 ALQRDGDRIA GLRVAITGSN SAPLMVPVDA LLGGNWDDAA AETLAQLVRK TSNVLRTTIT 310 320 GVKYRRRVLL AISRKVVDQL WEAR

References

[1]

"4-hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica -- prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins." Breese K., Fuchs G. Eur. J. Biochem. 251:916-923(1998) [PubMed: 9490068] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30 AND 169-185. Strain: DSM 6984 / K172.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ001830 Genomic DNA. Translation: CAA05039.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RM6	X-ray	1.60	B/E	1-324	[»]
1SB3	X-ray	2.20	B/E	1-324	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.3.99.20. 377.

Family and domain databases

InterPro

IPR017608. 4hydrxbenzoyl-CoA_Rdtase_bsu.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]

Gene3D

G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit.
G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit.
G3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit.

Pfam

PF00941. FAD_binding_5. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03195. 4hydrxCoA_B. 1 hit.

PROSITE

PS51387. FAD_PCMH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HCRB_THAAR

Accession

Primary (citable) accession number: O33820

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 61 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)