NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH FE(III), AND CHARACTERIZATION.
STRAIN=3E;
DOI=10.1074/jbc.M500666200; PubMed=15772073 [NCBI, ExPASy, EBI, Israel, Japan]
Ferraroni M., Seifert J., Travkin V.M., Thiel M., Kaschabek S., Scozzafava A., Golovleva L., Schloemann M., Briganti F.;
"Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation.";
J. Biol. Chem. 280:21144-21154(2005).

[2]

FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
STRAIN=3E;
DOI=10.1016/S0014-5793(97)00297-4; PubMed=9141483 [NCBI, ExPASy, EBI, Israel, Japan]
Travkin V.M., Jadan A.P., Briganti F., Scozzafava A., Golovleva L.A.;
"Characterization of an intradiol dioxygenase involved in the biodegradation of the chlorophenoxy herbicides 2,4-D and 2,4,5-T.";
FEBS Lett. 407:69-72(1997).

Comments

FUNCTION: Catalyzes the ortho-cleavage of the aromatic ring of hydroxyquinol.
CATALYTIC ACTIVITY: Benzene-1,2,4-triol + O₂ = 3-hydroxy-cis,cis-muconate.
COFACTOR: Binds 1 Fe(3+) ion per subunit.
ENZYME REGULATION: Inhibited by 3,5-dichlorocatechol, chlorohydroquinone and 4,5-dibromocatechol.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=1.2 µM for hydroxyquinol;
	V_max=55 µmol/min/mg enzyme with hydroxyquinol as substrate;
	Note=5-chlorohydroxyquinols and 6-chloro-chlorohydroxyquinols are also substrates;
pH dependence:	Optimum pH is 7.5;
Temperature dependence:	Optimum temperature is 50-55 degrees Celsius;

PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway; 3-oxoadipate from 3,4-dihydroxybenzoate: step 2/4 .
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.

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

AY822041; AAV71144.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1TMX; X-ray; 1.75 A; A/B=1-293.

[ExPASy / RCSB / EBI]

PDBsum

1TMX; -.

ModBase

Q5PXQ6.

Ontologies

GO:0018576;	Molecular function: catechol 1,2-dioxygenase activity (inferred from electronic annotation from InterPro).
GO:0008199;	Molecular function: ferric iron binding (inferred from electronic annotation from InterPro).
GO:0018581;	Molecular function: hydroxyquinol 1,2-dioxygenase activity (inferred from electronic annotation from EC).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0009712;	Biological process: catechol metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR007535; Catechol_dOase_N.
IPR000627; Intradiol_dOase_C.
IPR015889; Intradiol_dOase_core.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.130.10; Intradiol_dOase_core; 1.

Pfam

PF00775; Dioxygenase_C; 1.
PF04444; Dioxygenase_N; 1.
Pfam graphical view of domain structure.

PROSITE

PS00083; INTRADIOL_DIOXYGENAS; 1.

ProtoNet

Q5PXQ6.

Other

UniRef

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

Keywords

3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 293`	`293`	`Hydroxyquinol 1,2-dioxygenase.`	`PRO_0000085086`
`METAL`	`164 164`		`Iron.`
`METAL`	`197 197`		`Iron.`
`METAL`	`221 221`		`Iron.`
`METAL`	`223 223`		`Iron.`
`HELIX`	`7 23`	`17`
`TURN`	`24 26`	`3`
`HELIX`	`30 50`	`21`
`HELIX`	`54 70`	`17`
`HELIX`	`77 84`	`8`
`HELIX`	`87 95`	`9`
`STRAND`	`133 142`	`10`
`STRAND`	`152 156`	`5`
`HELIX`	`165 167`	`3`
`STRAND`	`168 170`	`3`
`STRAND`	`175 180`	`6`
`STRAND`	`185 192`	`8`
`HELIX`	`204 211`	`8`
`STRAND`	`221 227`	`7`
`STRAND`	`234 240`	`7`
`HELIX`	`244 247`	`4`
`HELIX`	`256 258`	`3`
`STRAND`	`263 265`	`3`
`HELIX`	`272 274`	`3`
`STRAND`	`281 285`	`5`
`STRAND`	`288 290`	`3`

Sequence information

Length: 293 AA [This is the length of the unprocessed precursor]

Molecular weight: 31967 Da [This is the MW of the unprocessed precursor]

CRC64: DEE403CF2AB8F5B0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTPVSAEQQ AREQDLVERV LRSFDATADP RLKQVMQALT RHLHAFLREV RLTEAEWETG 

        70         80         90        100        110        120 
IGFLTDAGHV TNERRQEFIL LSDVLGASMQ TIAMNNEAHG DATEATVFGP FFVEGSPRIE 

       130        140        150        160        170        180 
SGGDIAGGAA GEPCWVEGTV TDTDGNPVPD ARIEVWEADD DGFYDVQYDD DRTAARAHLL 

       190        200        210        220        230        240 
SGPDGGYAFW AITPTPYPIP HDGPVGRMLA ATGRSPMRAS HLHFMVTAPG RRTLVTHIFV 

       250        260        270        280        290 
EGDELLDRDS VFGVKDSLVK SFERQPAGAP TPGGREIDGP WSRVRFDIVL APA

Q5PXQ6 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