[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2254258 [NCBI, ExPASy, EBI, Israel, Japan] Nordlund I., Powlowski J., Shingler V.; "Complete nucleotide sequence and polypeptide analysis of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600."; J. Bacteriol. 172:6826-6833(1990).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=BH; Takeo M., Maeda Y., Okada H., Miyama K., Mori K., Ike M., Fujita M.; Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
[3]	STRUCTURE BY NMR. DOI=10.1021/bi9619233; PubMed=9012665 [NCBI, ExPASy, EBI, Israel, Japan] Qian H., Edlund U., Powlowski J., Shingler V., Sethson I.; "Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy."; Biochemistry 36:495-504(1997).

Comments

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

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

M60276; AAA25941.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D28864; BAA06016.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1HQI; NMR; -; A=1-90.

[ExPASy / RCSB / EBI]

PDBsum

1HQI; -.

ModBase

P19731.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12796; -.

Ontologies

GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0018662;	Molecular function: phenol 2-monooxygenase activity (inferred from electronic annotation from EC).
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

IPR003454; mOase_MmoB_DmpM.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.56.10; mOase_MmoB_DmpM; 1.

Pfam

PF02406; MmoB_DmpM; 1.
Pfam graphical view of domain structure.

ProDom

PD004249; MmoB_DmpM; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Other

P19731; -.

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

Keywords

3D-structure; Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Iron; Monooxygenase; NADP; Oxidoreductase; Plasmid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 90`	`90`	`Phenol hydroxylase P2 protein.`	`PRO_0000079943`
`STRAND`	`8 10`	`3`
`HELIX`	`14 25`	`12`
`STRAND`	`26 28`	`3`
`STRAND`	`43 48`	`6`
`HELIX`	`50 58`	`9`
`HELIX`	`60 62`	`3`
`HELIX`	`63 68`	`6`
`STRAND`	`69 72`	`4`
`STRAND`	`84 88`	`5`

Sequence information

Length: 90 AA [This is the length of the unprocessed precursor]

Molecular weight: 10491 Da [This is the MW of the unprocessed precursor]

CRC64: 32B3A5FB72664AED [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSLVYIAFQ DNDNARYVVE AIIQDNPHAV VQHHPAMIRI EAEKRLEIRR ETVEENLGRA 

        70         80         90 
WDVQEMLVDV ITIGGNVDED DDRFVLEWKN

P19731 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