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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)DescriptionActionsGraphical viewLength
    Binding sitei27FAD3 Publications1
    Binding sitei46FAD3 Publications1
    Binding sitei66FAD3 Publications1
    Binding sitei72FAD3 Publications1
    Binding sitei119FAD; via amide nitrogen and carbonyl oxygen3 Publications1
    Binding sitei152FAD3 Publications1
    Sitei337Transition state stabilizer2 Publications1
    Binding sitei446FAD; via amide nitrogen3 Publications1
    Binding sitei501NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi54 – 57FAD3 Publications4
    Nucleotide bindingi64 – 66NADP1 Publication3
    Nucleotide bindingi194 – 200NADP1 Publication7
    Nucleotide bindingi217 – 218NADP1 Publication2
    Nucleotide bindingi336 – 337NADP1 Publication2

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    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 databases

    DrugBankiDB03147. Flavin adenine dinucleotide.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002878851 – 542Phenylacetone monooxygenaseAdd BLAST542

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    STRINGi269800.Tfu_1490.

    Structurei

    Secondary structure

    1542
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi15 – 22Combined sources8
    Helixi26 – 37Combined sources12
    Beta strandi42 – 45Combined sources4
    Beta strandi47 – 51Combined sources5
    Helixi54 – 57Combined sources4
    Turni69 – 71Combined sources3
    Helixi78 – 83Combined sources6
    Beta strandi88 – 90Combined sources3
    Helixi93 – 106Combined sources14
    Helixi109 – 112Combined sources4
    Beta strandi119 – 125Combined sources7
    Turni126 – 129Combined sources4
    Beta strandi130 – 135Combined sources6
    Beta strandi140 – 148Combined sources9
    Helixi164 – 166Combined sources3
    Beta strandi169 – 173Combined sources5
    Helixi174 – 176Combined sources3
    Beta strandi188 – 192Combined sources5
    Helixi196 – 208Combined sources13
    Beta strandi209 – 218Combined sources10
    Beta strandi222 – 224Combined sources3
    Helixi232 – 239Combined sources8
    Helixi242 – 250Combined sources9
    Beta strandi252 – 256Combined sources5
    Turni265 – 267Combined sources3
    Helixi270 – 283Combined sources14
    Helixi286 – 290Combined sources5
    Turni293 – 297Combined sources5
    Helixi299 – 316Combined sources18
    Beta strandi317 – 319Combined sources3
    Helixi320 – 326Combined sources7
    Beta strandi333 – 336Combined sources4
    Beta strandi339 – 343Combined sources5
    Helixi344 – 347Combined sources4
    Beta strandi353 – 357Combined sources5
    Turni358 – 360Combined sources3
    Beta strandi363 – 366Combined sources4
    Beta strandi368 – 375Combined sources8
    Beta strandi377 – 379Combined sources3
    Beta strandi381 – 385Combined sources5
    Turni391 – 393Combined sources3
    Helixi394 – 397Combined sources4
    Beta strandi399 – 402Combined sources4
    Helixi404 – 406Combined sources3
    Helixi409 – 412Combined sources4
    Turni413 – 415Combined sources3
    Turni421 – 423Combined sources3
    Beta strandi431 – 435Combined sources5
    Helixi441 – 443Combined sources3
    Helixi446 – 466Combined sources21
    Beta strandi471 – 474Combined sources4
    Helixi476 – 490Combined sources15
    Helixi495 – 497Combined sources3
    Helixi499 – 501Combined sources3
    Beta strandi502 – 504Combined sources3
    Helixi521 – 533Combined sources13
    Beta strandi539 – 542Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi269800.Tfu_1490.

    Chemistry databases

    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

    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: November 2, 2016
    This is version 86 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.