[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=P4a; DOI=10.1099/mic.0.26260-0; PubMed=12949179 [NCBI, ExPASy, EBI, Israel, Japan] Hoffmann D., Kleinsteuber S., Mueller R.H., Babel W.; "A transposon encoding the complete 2,4-dichlorophenoxyacetic acid degradation pathway in the alkalitolerant strain Delftia acidovorans P4a."; Microbiology 149:2545-2556(2003).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 57-434. STRAIN=P4a; Hoffmann D., Kleinsteuber S., Mueller R.H., Babel W.; "Development and application of PCR primers for the detection of the tfd genes in Delftia acidovorans P4a involved in the degradation of 2,4-D."; Acta Biotechnol. 21:321-331(2001).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-432. STRAIN=MC1; DOI=10.1078/0944-5013-00089; PubMed=11572451 [NCBI, ExPASy, EBI, Israel, Japan] Mueller R.H., Kleinsteuber S., Babel W.; "Physiological and genetic characteristics of two bacterial strains utilizing phenoxypropionate and phenoxyacetate herbicides."; Microbiol. Res. 156:121-131(2001).
[4]	PROTEIN SEQUENCE OF 1-19. STRAIN=MC1; DOI=10.1099/mic.0.26774-0; PubMed=15073309 [NCBI, ExPASy, EBI, Israel, Japan] Benndorf D., Davidson I., Babel W.; "Regulation of catabolic enzymes during long-term exposure of Delftia acidovorans MC1 to chlorophenoxy herbicides."; Microbiology 150:1005-1014(2004).

Comments

FUNCTION: Transforms 2,4-dichlorophenol (2,4-DCP) into 3,5-dichlorocatechol (By similarity).
CATALYTIC ACTIVITY: 2,4-dichlorophenol + NADPH + O₂ = 3,5-dichlorocatechol + NADP⁺ + H₂O.
COFACTOR: FAD (By similarity).
PATHWAY: Xenobiotic degradation; 2,4-dichlorophenoxyacetic acid degradation .
SUBUNIT: Homotetramer (By similarity).
SIMILARITY: Belongs to the pheA/tfdB FAD monooxygenase 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

AY078159; AAM76774.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF176242; AAD55079.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q8KN28.

Ontologies

GO:0018666;	Molecular function: 2,4-dichlorophenol 6-monooxygenase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0019439;	Biological process: aromatic compound catabolic process (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

IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR002938; mOase_FAD_bd.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR003042; Rng_hydrolase.
Graphical view of domain structure.

Pfam

PF01494; FAD_binding_3; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00411; PNDRDTASEI.
PR00420; RNGMNOXGNASE.

ProtoNet

Q8KN28.

Other

UniRef

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

Keywords

Aromatic hydrocarbons catabolism; Direct protein sequencing; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 586`	`586`	`2,4-dichlorophenol 6-monooxygenase.`	`PRO_0000214050`
`NP_BIND`	`11 40`	`30`	`FAD (Potential).`
`NP_BIND`	`304 314`	`11`	`FAD (Potential).`
`CONFLICT`	`2 2`		`Missing (in Ref. 4; AA sequence).`
`CONFLICT`	`18 18`		`G -> A (in Ref. 4; AA sequence).`
`CONFLICT`	`195 195`		`M -> V (in Ref. 3; AAD55079).`

Sequence information

Length: 586 AA [This is the length of the unprocessed precursor]

Molecular weight: 64405 Da [This is the MW of the unprocessed precursor]

CRC64: 6BEE58517E7B860E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNEKATVIET DVLVVGSGPA GAASTLLLAT YGVKTLCVSK YATTSRTPRS HITNQRTMEV 

        70         80         90        100        110        120 
MRDLGLELEC EAMASPAELM GENVYCTSLV GDELGRVLTW GTHPQRRADY ELASPTHMCD 

       130        140        150        160        170        180 
LPQNLLEPIM INHAARRGAD VRFHTEFVSL KQDETGVTAT VRDHLLDRQY DIRAKYLIGA 

       190        200        210        220        230        240 
DGANSQVVDQ VGLPMEGKMG VSGSINVVFE ADLTKYVGHR PSVLYWVIQP GSSVGGLGIG 

       250        260        270        280        290        300 
VIRMVRPWNK WLCIWGYDIA GGPPDLNEAH ARQIVHSLLG DSTIPVKIES TSTWTVNDMY 

       310        320        330        340        350        360 
ATRLFDNRVF CMGDAVHRHP PTNGLGSNTS IQDAFNLCWK LSHVLQGKAG PELLATYNEE 

       370        380        390        400        410        420 
RAPVARQVVQ RANKSLGDFP PILAALGLFD TKDPEQMQRN IARLKEQSPE AQEQRAALRA 

       430        440        450        460        470        480 
AIDGTQYVYN AHGVEMNQRY QSAAIVPDGT PDPGFRRDSE LYHAHSGRPG APVPHVWVTR 

       490        500        510        520        530        540 
HGRRVSTLDL CGKGRFSLLS GIAGSPWVEA AVHAAESLGI DLDVHIIGPG QELEDLYGDF 

       550        560        570        580 
ARVREIEESG ALLVRPDNFI CWRAMRWQEG SGDELRAALK RVLSVH

Q8KN28 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