NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-19.
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: Binds 2 2Fe-2S clusters.
COFACTOR: FAD.
COFACTOR: Molybdenum.
ENZYME REGULATION: Inactivated by low concentrations of cyanide.
SUBUNIT: Heterohexamer of two alpha, two beta and two gamma subunits.
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.

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; CAA05037.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1RM6; X-ray; 1.60 A; C/F=1-161.	[ExPASy / RCSB / EBI]
1SB3; X-ray; 2.20 A; C/F=1-161.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1RM6; -.
1SB3; -.

ModBase

O33818.

Ontologies

GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
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:0005506;	Molecular function: iron ion 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

IPR002888; 2Fe-2S_bd.
IPR006058; 2Fe2S_fd_BS.
IPR017606; 4hydrxbenzoyl-CoA_Rdtase_gsu.
IPR001041; Ferredoxin.
Graphical view of domain structure.

Pfam

PF00111; Fer2; 1.
PF01799; Fer2_2; 1.
Pfam graphical view of domain structure.

ProDom

PD186071; 2Fe-2S_bind; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

O33818.

UniRef

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

Keywords

2Fe-2S; 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`	`1 161`	`161`	`4-hydroxybenzoyl-CoA reductase subunit gamma.`	`PRO_0000083927`
`DOMAIN`	`3 79`	`77`	`2Fe-2S ferredoxin-type.`
`METAL`	`41 41`		`Iron-sulfur (2Fe-2S) (Potential).`
`METAL`	`46 46`		`Iron-sulfur (2Fe-2S) (Potential).`
`METAL`	`49 49`		`Iron-sulfur (2Fe-2S) (Potential).`
`METAL`	`61 61`		`Iron-sulfur (2Fe-2S) (Potential).`
`METAL`	`100 100`		`Iron-sulfur (2Fe-2S) (Potential).`
`METAL`	`103 103`		`Iron-sulfur (2Fe-2S) (Potential).`
`METAL`	`135 135`		`Iron-sulfur (2Fe-2S) (Potential).`
`METAL`	`137 137`		`Iron-sulfur (2Fe-2S) (Potential).`
`STRAND`	`2 9`	`8`
`STRAND`	`12 19`	`8`
`HELIX`	`24 30`	`7`
`STRAND`	`41 46`	`6`
`STRAND`	`50 53`	`4`
`STRAND`	`56 59`	`4`
`HELIX`	`60 62`	`3`
`HELIX`	`65 68`	`4`
`STRAND`	`71 74`	`4`
`HELIX`	`76 78`	`3`
`STRAND`	`79 81`	`3`
`HELIX`	`87 94`	`8`
`HELIX`	`104 117`	`14`
`HELIX`	`123 129`	`7`
`TURN`	`130 132`	`3`
`STRAND`	`136 138`	`3`
`HELIX`	`141 155`	`15`

Sequence information

Length: 161 AA [This is the length of the unprocessed precursor]

Molecular weight: 17158 Da [This is the MW of the unprocessed precursor]

CRC64: CC2D8172F8EBA03B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKNILRLTLN GRAREDLVPD NMLLLDYLRE TVGLTGTKQG CDGGECGACT VLVDDRPRLA 

        70         80         90        100        110        120 
CSTLAHQVAG KKVETVESLA TQGTLSKLQA AFHEKLGTQC GFCTPGMIMA SEALLRKNPS 

       130        140        150        160 
PSRDEIKAAL AGNLCRCTGY VRSSKSVETA AAARLCEEGA R

O33818 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