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UniProtKB/Swiss-Prot entry Q47PU3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PAMO_THEFY
Primary accession number Q47PU3
Secondary accession numbers None
Integrated into Swiss-Prot on May 15, 2007
Sequence was last modified on September 13, 2005 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 27)
Name and origin of the protein
Protein name Phenylacetone monooxygenase
Synonyms PAMO
EC 1.14.13.92
Baeyer-Villiger monooxygenase
BVMO
Gene name
Name: pamO
OrderedLocusNames: Tfu_1490
From
Thermobifida fusca (strain YX) [TaxID: 269800] [HAMAP proteome]
Taxonomy Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; Streptosporangineae; Nocardiopsaceae; Thermobifida.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.01899-06; PubMed=17209016 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Genome sequence and analysis of the soil cellulolytic actinomycete Thermobifida fusca YX.";
J. Bacteriol. 189:2477-2486(2007).
[2]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1007/s00253-004-1749-5; PubMed=15599520 [NCBI, ExPASy, EBI, Israel, Japan]
Fraaije M.W., Wu J., Heuts D.P.H.M., van Hellemond E.W., Lutje Spelberg J.H., Janssen D.B.;
"Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining.";
Appl. Microbiol. Biotechnol. 66:393-400(2005).
[3]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FAD.
DOI=10.1073/pnas.0404538101; PubMed=15328411 [NCBI, ExPASy, EBI, Israel, Japan]
Malito E., Alfieri A., Fraaije M.W., Mattevi A.;
"Crystal structure of a Baeyer-Villiger monooxygenase.";
Proc. Natl. Acad. Sci. U.S.A. 101:13157-13162(2004).
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).
  • CATALYTIC ACTIVITY: Phenylacetone + NADPH + O2 = benzyl acetate + NADP+ + H2O.
  • COFACTOR: Binds 1 FAD per subunit.
  • 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;
  • SUBUNIT: Monomer.
  • SIMILARITY: Belongs to the FAD-binding 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
CP000088; AAZ55526.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_289549.1; -.
3D structure databases
PDB
1W4X; X-ray; 1.70 A; A=1-542.[ExPASy / RCSB / EBI]
PDBsum 1W4X; -.
ModBase Q47PU3.
Enzyme and pathway databases
BioCyc TFUS269800:TFU_1490-MON; -.
Family and domain databases
InterPro IPR006076; FAD-dep_OxRdtase.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR000960; Flavin_mOase.
IPR001100; Pyr_nuc-diS_OxRdtase.
Graphical view of domain structure.
Pfam PF01266; DAO; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00370; FMOXYGENASE.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS Q47PU3.
Genome annotation databases
GeneID 3581683; -.
GenomeReviews CP000088_GR; Tfu_1490.
KEGG tfu:Tfu_1490; -.
NMPDR fig|269800.4.peg.1774; -.
Phylogenomic databases
HOGENOM Q47PU3; -.
Genome annotation databases
CMR Q47PU3; Tfu_1490.
Other
ProtoNet Q47PU3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   542  542     Phenylacetone monooxygenase. PRO_0000287885
NP_BIND   26    27  2     FAD. 
NP_BIND   46    47  2     FAD. 
NP_BIND   54    55  2     FAD. 
NP_BIND   66    67  2     FAD. 
BINDING   72    72        FAD. 
BINDING   119   119        FAD; via amide nitrogen and carbonyl oxygen. 
BINDING   152   152        FAD. 
BINDING   446   446        FAD; via amide nitrogen. 
SITE   337   337  1     Transition state stabilizer (Potential). 
STRAND   15    22  8      
HELIX   26    37  12      
STRAND   42    45  4      
STRAND   47    51  5      
HELIX   54    57  4      
TURN   69    71  3      
HELIX   78    83  6      
STRAND   88    90  3      
HELIX   93   106  14      
HELIX   109   112  4      
STRAND   119   125  7      
TURN   126   129  4      
STRAND   130   135  6      
STRAND   140   148  9      
HELIX   164   166  3      
STRAND   169   173  5      
HELIX   174   176  3      
STRAND   188   192  5      
HELIX   196   208  13      
STRAND   209   218  10      
STRAND   222   224  3      
HELIX   232   239  8      
HELIX   242   250  9      
STRAND   252   256  5      
TURN   265   267  3      
HELIX   270   283  14      
HELIX   286   290  5      
TURN   293   297  5      
HELIX   299   316  18      
HELIX   320   326  7      
STRAND   333   336  4      
STRAND   339   343  5      
HELIX   344   347  4      
STRAND   353   357  5      
TURN   358   360  3      
STRAND   363   366  4      
STRAND   368   375  8      
STRAND   377   379  3      
STRAND   381   385  5      
HELIX   394   397  4      
STRAND   399   402  4      
HELIX   404   406  3      
HELIX   409   412  4      
TURN   413   415  3      
TURN   421   423  3      
STRAND   431   435  5      
HELIX   441   443  3      
HELIX   446   466  21      
STRAND   471   474  4      
HELIX   476   490  15      
HELIX   495   497  3      
HELIX   499   501  3      
STRAND   502   504  3      
HELIX   521   533  13      
Sequence information
Length: 542 AA [This is the length of the unprocessed precursor] Molecular weight: 61124 Da [This is the MW of the unprocessed precursor] CRC64: B24DF347F3D23D02 [This is a checksum on the sequence]
        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 

Q47PU3 in FASTA format

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