NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-30 AND 169-185.
STRAIN=DSM 6984 / K172;
PubMed=9490068 [NCBI, ExPASy, EBI, Israel, Japan]
Breese K., Fuchs G.;
"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.";
Eur. J. Biochem. 251:916-923(1998).

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.
COFACTOR: Iron-sulfur.
COFACTOR: Molybdenum.
ENZYME REGULATION: Inactivated by low concentrations of cyanide.
SUBUNIT: Heterohexamer of two alpha, two beta and two gamma subunits.
SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
SIMILARITY: To xanthine oxidases.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ001830; CAA05039.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1RM6; X-ray; 1.60 A; B/E=1-324.	[ExPASy / RCSB / EBI]
1SB3; X-ray; 2.20 A; B/E=1-324.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1RM6; -.
1SB3; -.

ModBase

O33820.

Ontologies

GO:0018525;	Molecular function: 4-hydroxybenzoyl-CoA reductase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051536;	Molecular function: iron-sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030151;	Molecular function: molybdenum ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR017608; 4hydrxbenzoyl-CoA_Rdtase_bsu.
IPR005107; CO_DHase_flav_C.
IPR016169; CO_DHase_flavot_FAD-bd_sub2.
IPR016167; FAD-bd_2_sub1.
IPR002346; Mopterin_DHase_FAD-bd.
Graphical view of domain structure.

Gene3D

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

Pfam

PF00941; FAD_binding_5; 1.
Pfam graphical view of domain structure.

PROSITE

PS51387; FAD_PCMH; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

O33820.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 324`	`324`	`4-hydroxybenzoyl-CoA reductase subunit beta.`	`PRO_0000083926`
`DOMAIN`	`2 217`	`216`	`FAD-binding PCMH-type.`
`METAL`	`117 117`		`Iron-sulfur (Potential).`
`METAL`	`122 122`		`Iron-sulfur (Potential).`
`METAL`	`138 138`		`Iron-sulfur (Potential).`
`METAL`	`146 146`		`Iron-sulfur (Potential).`
`METAL`	`155 155`		`Iron-sulfur (Potential).`
`CONFLICT`	`22 30`		`LAAEATLPL -> GTVPVAQLF (in Ref. 1; AA sequence).`
`STRAND`	`8 10`	`3`
`HELIX`	`15 21`	`7`
`STRAND`	`27 32`	`6`
`HELIX`	`36 41`	`6`
`STRAND`	`48 52`	`5`
`TURN`	`57 60`	`4`
`STRAND`	`62 64`	`3`
`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`
`STRAND`	`147 149`	`3`
`HELIX`	`163 169`	`7`
`STRAND`	`173 178`	`6`
`STRAND`	`181 186`	`6`
`HELIX`	`187 190`	`4`
`STRAND`	`206 212`	`7`
`STRAND`	`219 225`	`7`
`STRAND`	`227 231`	`5`
`STRAND`	`235 245`	`11`
`STRAND`	`248 262`	`15`
`HELIX`	`269 271`	`3`
`HELIX`	`278 291`	`14`
`STRAND`	`298 300`	`3`
`HELIX`	`302 322`	`21`

Sequence information

Length: 324 AA [This is the length of the unprocessed precursor]

Molecular weight: 34374 Da [This is the MW of the unprocessed precursor]

CRC64: C3C5ECAAD093F9DB [This is a checksum on the sequence]

        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

O33820 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools