[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]	PROBABLE FUNCTION, AND PROTEIN SEQUENCE OF 2-5. PubMed=2254259 [NCBI, ExPASy, EBI, Israel, Japan] Powlowski J., Shingler V.; "In vitro analysis of polypeptide requirements of multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600."; J. Bacteriol. 172:6834-6840(1990).

Comments

FUNCTION: Catabolizes phenol, and some of its methylated derivatives. P5 is required for growth on phenol, and for in vitro phenol hydroxylase activity.
FUNCTION: Probable electron transfer from NADPH, via FAD and the 2Fe-2S center, to the oxygenase activity site of the enzyme.
CATALYTIC ACTIVITY: Phenol + NADPH + O₂ = catechol + NADP⁺ + H₂O.
COFACTOR: Binds 1 FAD per subunit.
COFACTOR: Binds 1 2Fe-2S cluster per subunit.
PATHWAY: Aromatic compound metabolism; phenol degradation .
SUBUNIT: The multicomponent enzyme phenol hydroxylase is formed by P0, P1, P2, P3, P4 and P5 polypeptides.
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
SIMILARITY: Contains 1 FAD-binding FR-type domain.

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; AAA25944.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00235; 1FRR. [HSSP ENTRY / PDB]

ModBase

P19734.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12799; -.

Ontologies

GO:0005727;	Cellular component: extrachromosomal circular DNA (inferred from direct assay from UniProtKB).
GO:0018662;	Molecular function: phenol 2-monooxygenase activity (inferred from direct assay from UniProtKB).
GO:0046191;	Biological process: aerobic phenol catabolic process (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR006058; 2Fe2S_fd_BS.
IPR012675; b-grasp_ferredoxin-like.
IPR001041; Ferredoxin.
IPR008333; OxRdtase_FAD-bd.
IPR001433; OxRdtase_FAD/NAD_bd.
IPR001221; Phe_hydroxylase.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.20.30; Ferredoxin_fold; 1.

Pfam

PF00970; FAD_binding_6; 1.
PF00111; Fer2; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00410; PHEHYDRXLASE.

PROSITE

PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS51384; FAD_FR; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

2Fe-2S; Aromatic hydrocarbons catabolism; Direct protein sequencing; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Monooxygenase; NADP; Oxidoreductase; Plasmid; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 353`	`352`	`Phenol hydroxylase P5 protein.`	`PRO_0000189407`
`DOMAIN`	`3 93`	`91`	`2Fe-2S ferredoxin-type.`
`DOMAIN`	`102 201`	`100`	`FAD-binding FR-type.`
`METAL`	`37 37`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`42 42`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`45 45`		`Iron-sulfur (2Fe-2S) (By similarity).`
`METAL`	`77 77`		`Iron-sulfur (2Fe-2S) (By similarity).`

Sequence information

Length: 353 AA [This is the length of the unprocessed precursor]

Molecular weight: 38478 Da [This is the MW of the unprocessed precursor]

CRC64: 007E85A5DF189CD0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSYNVTIEPT GEVIEVEDGQ TILQAALRQG VWLPFACGHG TCATCKVQVV EGEVDIGEAS 

        70         80         90        100        110        120 
PFALMDIERD ERKVLACCAI PLSDLVIEAD VDADPDFLGH PVEDYRGVVS ALVDLSPTIK 

       130        140        150        160        170        180 
GLHIKLDRPM PFQAGQYVNL ALPGIDGTRA FSLANPPSRN DEVELHVRLV EGGAATGFIH 

       190        200        210        220        230        240 
KQLKVGDAVE LSGPYGQFFV RDSQAGDLIF IAGGSGLSSP QSMILDLLER GDTRRITLFQ 

       250        260        270        280        290        300 
GARNRAELYN CELFEELAAR HPNFSYVPAL NQANDDPEWQ GFKGFVHDAA KAHFDGRFGG 

       310        320        330        340        350 
QKAYLCGPPP MIDAAITTLM QGRLFERDIF MERFYTAADG AGESSRSALF KRI

P19734 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