Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q47PU3 (PAMO_THEFY)

Last modified December 16, 2008. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Phenylacetone monooxygenase
      Short name=PAMO
    EC=1.14.13.92
Alternative name(s):
    Baeyer-Villiger monooxygenase
      Short name=BVMO
Gene names
Name: pamO
Ordered Locus Names: Tfu_1490
OrganismThermobifida fusca (strain YX) [Complete proteome] [HAMAP]
Taxonomic identifier269800 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptosporangineae › Nocardiopsaceae › Thermobifida

Hide | Top

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Catalyzes a Baeyer-Villiger oxidation reaction, i.e., the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Is most efficient with phenylacetone as substrate, leading to the formation of benzyl acetate. Can also oxidize other aromatic ketones (benzylacetone, alpha-methylphenylacetone and 4-hydroxyacetophenone), some alipatic ketones (dodecan-2-one and bicyclohept-2-en-6-one) and sulfides (e.g. methyl 4-tolylsulfide). Ref.2

Catalytic activity

Phenylacetone + NADPH + O(2) = benzyl acetate + NADP(+) + H(2)O. Ref.2

Cofactor

Binds 1 FAD per subunit. Ref.2

Subunit structure

Monomer. Ref.2

Sequence similarities

Belongs to the FAD-binding monooxygenase family.

Biophysicochemical properties

Kinetic parameters:

KM=3 µM for NADPH

KM=59 µM for phenylacetone

KM=360 µM for benzylacetone

KM=830 µM for alpha-methylphenylacetone

KM=2.2 mM for 4-hydroxyacetophenone

KM=260 µM for 2-dodecanone

KM=15 mM for bicyclohept-2-en-6-one

KM=860 µM for methyl 4-tolylsulfide

pH dependence:

Optimum pH is 8.0.

Temperature dependence:

Thermostable. Displays an activity half-life of 1 day at 52 degrees Celsius.

Hide | Top

Ontologies

Keywords

   LigandFAD
Flavoprotein
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionphenylacetone monooxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542Phenylacetone monooxygenase
PRO_0000287885

Regions

Nucleotide binding26 – 272FAD
Nucleotide binding46 – 472FAD
Nucleotide binding54 – 552FAD
Nucleotide binding66 – 672FAD

Sites

Binding site721FAD
Binding site1191FAD; via amide nitrogen and carbonyl oxygen
Binding site1521FAD
Binding site4461FAD; via amide nitrogen
Site3371Transition state stabilizer Potential

Secondary structure

1 ..................................................................................................... 542
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q47PU3-1 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: B24DF347F3D23D02

FASTA54261,124
        10         20         30         40         50         60 
MAGQTTVDSR RQPPEEVDVL VVGAGFSGLY ALYRLRELGR SVHVIETAGD VGGVWYWNRY 

        70         80         90        100        110        120 
PGARCDIESI EYCYSFSEEV LQEWNWTERY ASQPEILRYI NFVADKFDLR SGITFHTTVT 

       130        140        150        160        170        180 
AAAFDEATNT WTVDTNHGDR IRARYLIMAS GQLSVPQLPN FPGLKDFAGN LYHTGNWPHE 

       190        200        210        220        230        240 
PVDFSGQRVG VIGTGSSGIQ VSPQIAKQAA ELFVFQRTPH FAVPARNAPL DPEFLADLKK 

       250        260        270        280        290        300 
RYAEFREESR NTPGGTHRYQ GPKSALEVSD EELVETLERY WQEGGPDILA AYRDILRDRD 

       310        320        330        340        350        360 
ANERVAEFIR NKIRNTVRDP EVAERLVPKG YPFGTKRLIL EIDYYEMFNR DNVHLVDTLS 

       370        380        390        400        410        420 
APIETITPRG VRTSEREYEL DSLVLATGFD ALTGALFKID IRGVGNVALK EKWAAGPRTY 

       430        440        450        460        470        480 
LGLSTAGFPN LFFIAGPGSP SALSNMLVSI EQHVEWVTDH IAYMFKNGLT RSEAVLEKED 

       490        500        510        520        530        540 
EWVEHVNEIA DETLYPMTAS WYTGANVPGK PRVFMLYVGG FHRYRQICDE VAAKGYEGFV 


LT

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX."
Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B., Kyrpides N.
J. Bacteriol. 189:2477-2486(2007) [PubMed: 17209016] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining."
Fraaije M.W., Wu J., Heuts D.P.H.M., van Hellemond E.W., Lutje Spelberg J.H., Janssen D.B.
Appl. Microbiol. Biotechnol. 66:393-400(2005) [PubMed: 15599520] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[3]"Crystal structure of a Baeyer-Villiger monooxygenase."
Malito E., Alfieri A., Fraaije M.W., Mattevi A.
Proc. Natl. Acad. Sci. U.S.A. 101:13157-13162(2004) [PubMed: 15328411] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FAD.

Hide | Top

Cross-references

Sequence databases

CP000088 Genomic DNA. Translation: AAZ55526.1.
RefSeqYP_289549.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1W4XX-ray1.70A1-542[»]
ModBaseSearch...

Genome annotation databases

GeneID3581683.
GenomeReviewsGene locus Tfu_1490 in contig CP000088_GR.
KEGGtfu:Tfu_1490.
NMPDRfig|269800.4.peg.1774.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ47PU3.

Enzyme and pathway databases

BioCycTFUS269800:TFU_1490-MON.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000960. Flavin_mOase.
IPR001100. Pyr_nuc-diS_OxRdtase.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00370. FMOXYGENASE.
PR00411. PNDRDTASEI.
ProDomPD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Hide | Top

Entry information

Entry namePAMO_THEFY
AccessionPrimary (citable) accession number: Q47PU3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: September 13, 2005
Last modified: December 16, 2008
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)