[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=PHEA-2; DOI=10.1007/s00284-002-3840-4; PubMed=12732969 [NCBI, ExPASy, EBI, Israel, Japan] Xu Y., Chen M., Zhang W., Lin M.; "Genetic organization of genes encoding phenol hydroxylase, benzoate 1,2-dioxygenase alpha subunit and its regulatory proteins in Acinetobacter calcoaceticus PHEA-2."; Curr. Microbiol. 46:235-240(2003).
[2]	PROTEIN SEQUENCE OF 2-16. STRAIN=69-V; Benndorf D., Loffhagen N., Hartig C., Babel W.; "Growth on phenol at chemostress levels amplifies the expression of the phenol degradation pathway in Acinetobacter calcoaceticus."; Eng. Life Sci. 4:38-42(2004).

Comments

FUNCTION: Catabolizes phenol, and some of its methylated derivatives. P1 is required for growth on phenol, and for in vitro phenol hydroxylase activity (By similarity).
CATALYTIC ACTIVITY: Phenol + NADPH + O₂ = catechol + NADP⁺ + H₂O.
COFACTOR: FAD (By similarity).
COFACTOR: Fe(2+) (By similarity).
PATHWAY: Aromatic compound metabolism; phenol degradation .
SUBUNIT: The multicomponent enzyme phenol hydroxylase is formed by P0, P1, P2, P3, P4 and P5 polypeptides (By similarity).
INDUCTION: By phenol.

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

AJ564846; CAD92312.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q7WTJ6.

Ontologies

GO:0018662;	Molecular function: phenol 2-monooxygenase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0046191;	Biological process: aerobic phenol catabolic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR012078; MP_mOase_hydro.
IPR003430; Phenol_Hydrox.
IPR012348; Ribncl_red_rel.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.620.20; Ribncl_red_rel; 1.

Pfam

PF02332; Phenol_Hydrox; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000040; MMOH_comp; 1.

Other

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 332`	`331`	`Phenol hydroxylase P1 protein.`	`PRO_0000079941`

Sequence information

Length: 332 AA [This is the length of the unprocessed precursor]

Molecular weight: 38226 Da [This is the MW of the unprocessed precursor]

CRC64: FCAE249C720A0BA6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTLEIKTSNV EPIRQNYAYI ERRFGSKPAT RYQEVSFDVQ AETNFHYRPL WKPEKTLNDK 

        70         80         90        100        110        120 
THTALQMQDW YAFKDPRQFY YGTYVQHRAR LQDTAESNFA FFEKRQLAEH LSNEVKAKVI 

       130        140        150        160        170        180 
ECLLPFRHVE QTANLHMMSG SAYGYGTVLT QACIYAAMDH LGIAQYISRI GLALDGNSGD 

       190        200        210        220        230        240 
SLQQAKQAWM QHPAWQGLRR LCEESLTEQD YFKLFLLQNL VIDGFVTELV YQQFDQWLVS 

       250        260        270        280        290        300 
QNARDLAMLT EFMKDTLGDL RKWSDTVIKT AAAESDHNKQ LLNEWFTESL AQVKAAFTPW 

       310        320        330 
ATAALTVDAV DQAEQAVIER AKKLGLQPLT NA

Q7WTJ6 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