NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 19070 / V49;
DOI=10.1023/A:1001784702230; PubMed=10068799 [NCBI, ExPASy, EBI, Israel, Japan]
Powell J.A., Archer J.A.;
"Molecular characterisation of a Rhodococcus ohp operon.";
Antonie Van Leeuwenhoek 74:175-188(1998).

Comments

FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively. Also catalyzes the cleavage of catechol.
CATALYTIC ACTIVITY: 3-(2,3-dihydroxyphenyl)propanoate + O₂ = 2-hydroxy-6-oxonona-2,4-diene-1,9-dioate.
CATALYTIC ACTIVITY: 2,3-dihydroxicinnamic acid + O₂ = 2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate.
COFACTOR: Fe(2+) ion (By similarity).

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=30 µM for 3-(2,3-dihydroxyphenyl) propionic acid (at pH 8.1 and 8 degrees Celsius);
	K_M=47 µM for catechol (at pH 8.1 and 8 degrees Celsius);
	K_M=62 µM for 3-methylcatechol (at pH 8.1 and 8 degrees Celsius);

PATHWAY: Aromatic compound metabolism; 3-phenylpropionic acid degradation .
SUBUNIT: Homotetramer (By similarity).
SIMILARITY: Belongs to the ligB/mhpB extradiol 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

AF274045; AAF81826.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q9KH19.

Ontologies

GO:0008669;	Molecular function: 2,3-dihydroxy-phenylpropionate 1,2-dioxygenase activity (inferred from electronic annotation from HAMAP).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01653; -; 1.
PBIL [Tree]

InterPro

IPR004183; Xdiol_dOase_3B.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.830.10; Xdiol_dOase_3B; 1.

Pfam

PF02900; LigB; 1.
Pfam graphical view of domain structure.

Other

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

Keywords

Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 314`	`314`	`2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase.`	`PRO_0000337667`
`ACT_SITE`	`115 115`		`Proton donor (By similarity).`
`ACT_SITE`	`179 179`		`Proton acceptor (By similarity).`

Sequence information

Length: 314 AA [This is the length of the unprocessed precursor]

Molecular weight: 33916 Da [This is the MW of the unprocessed precursor]

CRC64: C919C10770527E64 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPVALCAMSH SPLMGRNDPE QEVIDAVDAA FDHARRFVAD FAPDLIVIFA PDHYNGVFYD 

        70         80         90        100        110        120 
LLPPFCIGAA AQSVGDYGTE AGPLDVDRDA AYAVARDVLD SGIDVAFSER MHVDHGFAQA 

       130        140        150        160        170        180 
LQLLVGSITA VPTVPIFINS VAEPLGPVSR VRLLGEAVGR AAAKLDKRVL FVGSGGLSHD 

       190        200        210        220        230        240 
PPVPQFATAP EEVRERLIDG RNPSAAERDA REQRVITAGR DFAAGTAAIQ PLNPEWDRHL 

       250        260        270        280        290        300 
LDVLASGDLE QIDAWTNDWF VEQAGHSSHE VRTWIAAYAA MSAAGKYRVT STFYREIHEW 

       310 
IAGFGITTAV AVDE

Q9KH19 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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