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Protein

Phenylacetone monooxygenase

Gene

pamO

Organism
Thermobifida fusca (strain YX)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 aliphatic ketones (dodecan-2-one and bicyclohept-2-en-6-one) and sulfides (e.g. methyl 4-tolylsulfide).1 Publication

Catalytic activityi

Phenylacetone + NADPH + O2 = benzyl acetate + NADP+ + H2O.1 Publication

Cofactori

FAD1 PublicationNote: Binds 1 FAD per subunit.1 Publication

Kineticsi

  1. KM=3 µM for NADPH1 Publication
  2. KM=59 µM for phenylacetone1 Publication
  3. KM=360 µM for benzylacetone1 Publication
  4. KM=830 µM for alpha-methylphenylacetone1 Publication
  5. KM=2.2 mM for 4-hydroxyacetophenone1 Publication
  6. KM=260 µM for 2-dodecanone1 Publication
  7. KM=15 mM for bicyclohept-2-en-6-one1 Publication
  8. KM=860 µM for methyl 4-tolylsulfide1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Temperature dependencei

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei27 – 271FAD3 Publications
    Binding sitei46 – 461FAD3 Publications
    Binding sitei66 – 661FAD3 Publications
    Binding sitei72 – 721FAD3 Publications
    Binding sitei119 – 1191FAD; via amide nitrogen and carbonyl oxygen3 Publications
    Binding sitei152 – 1521FAD3 Publications
    Sitei337 – 3371Transition state stabilizer2 Publications
    Binding sitei446 – 4461FAD; via amide nitrogen3 Publications
    Binding sitei501 – 5011NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi54 – 574FAD3 Publications
    Nucleotide bindingi64 – 663NADP1 Publication
    Nucleotide bindingi194 – 2007NADP1 Publication
    Nucleotide bindingi217 – 2182NADP1 Publication
    Nucleotide bindingi336 – 3372NADP1 Publication

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciTFUS269800:GI42-1498-MONOMER.
    BRENDAi1.14.13.92. 6298.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenylacetone monooxygenase (EC:1.14.13.92)
    Short name:
    PAMO
    Alternative name(s):
    Baeyer-Villiger monooxygenase
    Short name:
    BVMO
    Gene namesi
    Name:pamO
    Ordered Locus Names:Tfu_1490
    OrganismiThermobifida fusca (strain YX)
    Taxonomic identifieri269800 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptosporangialesNocardiopsaceaeThermobifida
    Proteomesi
    • UP000000434 Componenti: Chromosome

    Pathology & Biotechi

    Chemistry

    DrugBankiDB03147. Flavin adenine dinucleotide.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 542542Phenylacetone monooxygenasePRO_0000287885Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    STRINGi269800.Tfu_1490.

    Structurei

    Secondary structure

    1
    542
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 228Combined sources
    Helixi26 – 3712Combined sources
    Beta strandi42 – 454Combined sources
    Beta strandi47 – 515Combined sources
    Helixi54 – 574Combined sources
    Turni69 – 713Combined sources
    Helixi78 – 836Combined sources
    Beta strandi88 – 903Combined sources
    Helixi93 – 10614Combined sources
    Helixi109 – 1124Combined sources
    Beta strandi119 – 1257Combined sources
    Turni126 – 1294Combined sources
    Beta strandi130 – 1356Combined sources
    Beta strandi140 – 1489Combined sources
    Helixi164 – 1663Combined sources
    Beta strandi169 – 1735Combined sources
    Helixi174 – 1763Combined sources
    Beta strandi188 – 1925Combined sources
    Helixi196 – 20813Combined sources
    Beta strandi209 – 21810Combined sources
    Beta strandi222 – 2243Combined sources
    Helixi232 – 2398Combined sources
    Helixi242 – 2509Combined sources
    Beta strandi252 – 2565Combined sources
    Turni265 – 2673Combined sources
    Helixi270 – 28314Combined sources
    Helixi286 – 2905Combined sources
    Turni293 – 2975Combined sources
    Helixi299 – 31618Combined sources
    Beta strandi317 – 3193Combined sources
    Helixi320 – 3267Combined sources
    Beta strandi333 – 3364Combined sources
    Beta strandi339 – 3435Combined sources
    Helixi344 – 3474Combined sources
    Beta strandi353 – 3575Combined sources
    Turni358 – 3603Combined sources
    Beta strandi363 – 3664Combined sources
    Beta strandi368 – 3758Combined sources
    Beta strandi377 – 3793Combined sources
    Beta strandi381 – 3855Combined sources
    Turni391 – 3933Combined sources
    Helixi394 – 3974Combined sources
    Beta strandi399 – 4024Combined sources
    Helixi404 – 4063Combined sources
    Helixi409 – 4124Combined sources
    Turni413 – 4153Combined sources
    Turni421 – 4233Combined sources
    Beta strandi431 – 4355Combined sources
    Helixi441 – 4433Combined sources
    Helixi446 – 46621Combined sources
    Beta strandi471 – 4744Combined sources
    Helixi476 – 49015Combined sources
    Helixi495 – 4973Combined sources
    Helixi499 – 5013Combined sources
    Beta strandi502 – 5043Combined sources
    Helixi521 – 53313Combined sources
    Beta strandi539 – 5424Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W4XX-ray1.70A1-542[»]
    2YLRX-ray2.26A1-542[»]
    2YLSX-ray2.26A1-542[»]
    2YLTX-ray2.65A1-542[»]
    2YLWX-ray2.90A1-542[»]
    2YLXX-ray2.20A1-542[»]
    2YLZX-ray2.00A1-542[»]
    2YM1X-ray2.28A1-542[»]
    2YM2X-ray2.70A1-542[»]
    4C74X-ray1.97A1-542[»]
    4C77X-ray2.70A1-542[»]
    4D03X-ray1.81A1-542[»]
    4D04X-ray1.75A1-542[»]
    4OVIX-ray1.87A1-542[»]
    ProteinModelPortaliQ47PU3.
    SMRiQ47PU3. Positions 10-542.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ47PU3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FAD-binding monooxygenase family.Curated

    Phylogenomic databases

    eggNOGiENOG4107S2E. Bacteria.
    COG2072. LUCA.
    HOGENOMiHOG000204545.
    KOiK18229.
    OMAiFQRTANF.
    OrthoDBiPOG091H08T2.

    Family and domain databases

    Gene3Di3.50.50.60. 4 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 3 hits.

    Sequencei

    Sequence statusi: Complete.

    Q47PU3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAGQTTVDSR RQPPEEVDVL VVGAGFSGLY ALYRLRELGR SVHVIETAGD
    60 70 80 90 100
    VGGVWYWNRY PGARCDIESI EYCYSFSEEV LQEWNWTERY ASQPEILRYI
    110 120 130 140 150
    NFVADKFDLR SGITFHTTVT AAAFDEATNT WTVDTNHGDR IRARYLIMAS
    160 170 180 190 200
    GQLSVPQLPN FPGLKDFAGN LYHTGNWPHE PVDFSGQRVG VIGTGSSGIQ
    210 220 230 240 250
    VSPQIAKQAA ELFVFQRTPH FAVPARNAPL DPEFLADLKK RYAEFREESR
    260 270 280 290 300
    NTPGGTHRYQ GPKSALEVSD EELVETLERY WQEGGPDILA AYRDILRDRD
    310 320 330 340 350
    ANERVAEFIR NKIRNTVRDP EVAERLVPKG YPFGTKRLIL EIDYYEMFNR
    360 370 380 390 400
    DNVHLVDTLS APIETITPRG VRTSEREYEL DSLVLATGFD ALTGALFKID
    410 420 430 440 450
    IRGVGNVALK EKWAAGPRTY LGLSTAGFPN LFFIAGPGSP SALSNMLVSI
    460 470 480 490 500
    EQHVEWVTDH IAYMFKNGLT RSEAVLEKED EWVEHVNEIA DETLYPMTAS
    510 520 530 540
    WYTGANVPGK PRVFMLYVGG FHRYRQICDE VAAKGYEGFV LT
    Length:542
    Mass (Da):61,124
    Last modified:September 13, 2005 - v1
    Checksum:iB24DF347F3D23D02
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000088 Genomic DNA. Translation: AAZ55526.1.
    RefSeqiWP_011291921.1. NC_007333.1.

    Genome annotation databases

    EnsemblBacteriaiAAZ55526; AAZ55526; Tfu_1490.
    KEGGitfu:Tfu_1490.
    PATRICi23903546. VBITheFus33945_1599.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000088 Genomic DNA. Translation: AAZ55526.1.
    RefSeqiWP_011291921.1. NC_007333.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W4XX-ray1.70A1-542[»]
    2YLRX-ray2.26A1-542[»]
    2YLSX-ray2.26A1-542[»]
    2YLTX-ray2.65A1-542[»]
    2YLWX-ray2.90A1-542[»]
    2YLXX-ray2.20A1-542[»]
    2YLZX-ray2.00A1-542[»]
    2YM1X-ray2.28A1-542[»]
    2YM2X-ray2.70A1-542[»]
    4C74X-ray1.97A1-542[»]
    4C77X-ray2.70A1-542[»]
    4D03X-ray1.81A1-542[»]
    4D04X-ray1.75A1-542[»]
    4OVIX-ray1.87A1-542[»]
    ProteinModelPortaliQ47PU3.
    SMRiQ47PU3. Positions 10-542.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi269800.Tfu_1490.

    Chemistry

    DrugBankiDB03147. Flavin adenine dinucleotide.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAZ55526; AAZ55526; Tfu_1490.
    KEGGitfu:Tfu_1490.
    PATRICi23903546. VBITheFus33945_1599.

    Phylogenomic databases

    eggNOGiENOG4107S2E. Bacteria.
    COG2072. LUCA.
    HOGENOMiHOG000204545.
    KOiK18229.
    OMAiFQRTANF.
    OrthoDBiPOG091H08T2.

    Enzyme and pathway databases

    BioCyciTFUS269800:GI42-1498-MONOMER.
    BRENDAi1.14.13.92. 6298.

    Miscellaneous databases

    EvolutionaryTraceiQ47PU3.

    Family and domain databases

    Gene3Di3.50.50.60. 4 hits.
    InterProiIPR023753. FAD/NAD-binding_dom.
    [Graphical view]
    SUPFAMiSSF51905. SSF51905. 3 hits.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPAMO_THEFY
    AccessioniPrimary (citable) accession number: Q47PU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: September 13, 2005
    Last modified: September 7, 2016
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.