[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-14. STRAIN=ATCC 39723 / DSM 6824 / L-1; PubMed=7678243 [NCBI, ExPASy, EBI, Israel, Japan] Orser C.S., Lange C.C., Xun L., Zahrt T.C., Schneider B.J.; "Cloning, sequence analysis, and expression of the Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli."; J. Bacteriol. 175:411-416(1993).
[2]	SEQUENCE REVISION TO 536, FUNCTION, AND INDUCTION. STRAIN=ATCC 39723 / DSM 6824 / L-1; DOI=10.1128/JB.184.17.4672-4680.2002; PubMed=12169590 [NCBI, ExPASy, EBI, Israel, Japan] Cai M., Xun L.; "Organization and regulation of pentachlorophenol-degrading genes in Sphingobium chlorophenolicum ATCC 39723."; J. Bacteriol. 184:4672-4680(2002).

Comments

FUNCTION: Dechlorination of pentachlorophenol to tetrachlorohydroquinone. Removes also hydrogen and nitro, amino, and cyano groups from benzene ring at the para position in relation to the hydroxyl of phenol.
CATALYTIC ACTIVITY: Pentachlorophenol + 2 NADPH + O₂ = 2,3,5,6-tetrachlorohydroquinone + 2 NADP⁺ + chloride + H₂O.
CATALYTIC ACTIVITY: 2,3,5,6-tetrachlorophenol + NADPH + O₂ = 2,3,5,6-tetrachlorohydroquinone + NADP⁺ + H₂O.
COFACTOR: FAD (By similarity).
PATHWAY: Xenobiotic degradation; pentachlorophenol degradation .
INDUCTION: By polychlorinated phenols.
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

U12290; AAF15368.2; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

P42535.

Family and domain databases

InterPro

IPR000759; Adrndx_reductase.
IPR002938; mOase_FAD_bd.
IPR003042; Rng_hydrolase.
Graphical view of domain structure.

Pfam

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

PRINTS

PR00419; ADXRDTASE.
PR00420; RNGMNOXGNASE.

Other

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`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 538`	`537`	`Pentachlorophenol 4-monooxygenase.`	`PRO_0000214044`
`NP_BIND`	`16 45`	`30`	`FAD (Potential).`
`NP_BIND`	`288 298`	`11`	`FAD (Potential).`

Sequence information

Length: 538 AA [This is the length of the unprocessed precursor]

Molecular weight: 59992 Da [This is the MW of the unprocessed precursor]

CRC64: CB545A9A1DCE8AB9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTYPINAPG QSADAAVLIV GGGPTGLIAA NELLRRGVSC RMIDRLPVAH QTSKSCTIHA 

        70         80         90        100        110        120 
RSMEMMEHIG IAARYIETGV RSNGFTFNFE NTDANALLDF SVLPGRYPFI TIYNQNETER 

       130        140        150        160        170        180 
VLRHDLEATY SFQPEWGTQL LALNQDENGI RADLRLKDGT KQTISPRWVI GADGVRSRVR 

       190        200        210        220        230        240 
ECLGIAYEGE DYEENVLQMM DVGIQDFEAG DDWIHYFIGQ DKFVFVTKLP GSNYRVIISD 

       250        260        270        280        290        300 
LGGANKSNLE ETREAFQGYL SSFDDHATLD EPRWATKWRV WKRMATAYRK GNVFLAGDAA 

       310        320        330        340        350        360 
HCHSPSGGSG MNVGMQDAFN LGWKIAMVER GEAKPDLLDT YHTERTPVAQ QLLEGTHAMH 

       370        380        390        400        410        420 
EIIMGHGKGL TDRIELTQAP GWHDAATYRV SGMSYNYRDQ LVSFNDDRLA GPSAGDRIPD 

       430        440        450        460        470        480 
AELAPRIRLF DLVRNTRPTL LVAPATEAEV AEAEKLRDLI REQWPLVKPV LVRPQGSEES 

       490        500        510        520        530 
IEGDVHVDSY GQLKREWGDN AKGWAALLRP DNYIHARAGL DRGDLLVQAI DAMLVRCA

P42535 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