Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phenylalanine 2-monooxygenase precursor

Gene
N/A
Organism
Pseudomonas sp.
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes both oxygenative decarboxylation and oxidative deamination, depending on the substrate used. Has high activity for L-Phe and L-Tyr, but relatively low activities for L-Met and L-Trp. L-Phe is mainly oxygenated and L-Met is mainly oxidized.6 Publications

Catalytic activityi

L-phenylalanine + O2 = 2-phenylacetamide + CO2 + H2O.3 Publications

Cofactori

FAD2 PublicationsNote: Binds 2 FAD per tetramer.2 Publications

Kineticsi

  1. KM=11.1 µM for L-Phe (for the oxygenation reaction)3 Publications
  2. KM=13.3 µM for L-Phe (for the oxidation reaction)3 Publications
  3. KM=4 mM for L-Tyr3 Publications
  4. KM=2.2 mM for L-Met3 Publications
  5. KM=1.96 mM for O2 (for the oxygenation reaction with L-Phe as cosubstrate)3 Publications
  6. KM=2.04 mM for O2 (for the oxidation reaction with L-Phe as cosubstrate)3 Publications
  7. KM=3.145 mM for for O2 (with L-Tyr as cosubstrate)3 Publications
  8. KM=1.258 mM for for O2 (with L-Met as cosubstrate)3 Publications

    pH dependencei

    Optimum pH is 6-9 for the oxygenation reaction and 10.5 for the oxidation reaction.3 Publications

    Temperature dependencei

    Optimum temperature is 45 degrees Celsius for the oxygenation reaction and 65 degrees Celsius for the oxygenation reaction. Stable up to 70 degrees Celsius.3 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei2FAD; via amide nitrogen1 Publication1
    Binding sitei68FAD; via amide nitrogen1 Publication1
    Binding sitei120FAD1 Publication1
    Binding sitei144Substrate1
    Binding sitei375FAD; via amide nitrogen and carbonyl oxygen1 Publication1
    Binding sitei537Substrate1
    Binding sitei660Substrate; via carbonyl oxygen1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi95 – 96FAD1 Publication2
    Nucleotide bindingi141 – 144FAD1 Publication4
    Nucleotide bindingi652 – 653FAD1 Publication2
    Nucleotide bindingi660 – 662FAD1 Publication3

    GO - Molecular functioni

    • nucleotide binding Source: UniProtKB-KW
    • phenylalanine 2-monooxygenase activity Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi1.13.12.9. 5085.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenylalanine 2-monooxygenase precursor (EC:1.13.12.9)
    Short name:
    proPAO
    Alternative name(s):
    L-phenylalanine oxidase (deaminating and decarboxylating)
    Short name:
    PAO
    Cleaved into the following 2 chains:
    OrganismiPseudomonas sp.
    Taxonomic identifieri306 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi143M → A: Reduces catalytic efficiency 10-fold. 1 Publication1
    Mutagenesisi144R → A: Abolishes catalytic activity. 1 Publication1
    Mutagenesisi144R → K: Reduces catalytic activity 400-fold. 1 Publication1
    Mutagenesisi479K → A: Reduces catalytic efficiency 200-fold. 1 Publication1
    Mutagenesisi537Y → A: Abolishes catalytic activity. 1 Publication1
    Mutagenesisi537Y → F: Reduces catalytic activity 17-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    PropeptideiPRO_00004242221 – 15Removed in mature form; occupies the channel of the substrate amino acid from the outside of the protein to the interior flavin ring in the precursor1 PublicationAdd BLAST15
    ChainiPRO_500005113216 – 107Phenylalanine 2-monooxygenase alpha subunitAdd BLAST92
    PropeptideiPRO_0000424223108 – 109Linker peptide1 Publication2
    ChainiPRO_0000424224110 – 714Phenylalanine 2-monooxygenase beta subunitAdd BLAST605

    Post-translational modificationi

    Proteolytically cleaved to yield the active enzyme. Cleavage of the linkage between the 2 subunits causes reshaping of the oxygen channel and the hydrophobic environment around the flavin ring. Removal of the prosequence causes opening of the amino acid channel.1 Publication

    Keywords - PTMi

    Zymogen

    Interactioni

    Subunit structurei

    Heterotetramer composed of 2 alpha and 2 beta subunits.2 Publications

    Structurei

    Secondary structure

    1714
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi22 – 28Combined sources7
    Turni29 – 31Combined sources3
    Helixi35 – 37Combined sources3
    Helixi42 – 45Combined sources4
    Beta strandi55 – 63Combined sources9
    Helixi67 – 80Combined sources14
    Beta strandi88 – 94Combined sources7
    Helixi101 – 103Combined sources3
    Beta strandi121 – 126Combined sources6
    Helixi131 – 133Combined sources3
    Beta strandi135 – 139Combined sources5
    Helixi150 – 160Combined sources11
    Beta strandi177 – 181Combined sources5
    Beta strandi184 – 191Combined sources8
    Helixi193 – 195Combined sources3
    Beta strandi196 – 198Combined sources3
    Helixi202 – 214Combined sources13
    Beta strandi218 – 221Combined sources4
    Helixi233 – 240Combined sources8
    Helixi247 – 255Combined sources9
    Helixi257 – 265Combined sources9
    Helixi270 – 283Combined sources14
    Helixi290 – 292Combined sources3
    Helixi296 – 310Combined sources15
    Beta strandi312 – 315Combined sources4
    Helixi318 – 320Combined sources3
    Helixi325 – 333Combined sources9
    Turni334 – 337Combined sources4
    Beta strandi339 – 341Combined sources3
    Beta strandi343 – 346Combined sources4
    Helixi348 – 361Combined sources14
    Turni362 – 364Combined sources3
    Beta strandi365 – 371Combined sources7
    Beta strandi373 – 380Combined sources8
    Beta strandi382 – 385Combined sources4
    Beta strandi388 – 394Combined sources7
    Beta strandi399 – 409Combined sources11
    Helixi413 – 420Combined sources8
    Beta strandi421 – 423Combined sources3
    Beta strandi428 – 434Combined sources7
    Helixi436 – 438Combined sources3
    Beta strandi443 – 449Combined sources7
    Helixi459 – 470Combined sources12
    Beta strandi477 – 485Combined sources9
    Helixi486 – 490Combined sources5
    Beta strandi504 – 507Combined sources4
    Turni508 – 511Combined sources4
    Beta strandi512 – 518Combined sources7
    Beta strandi529 – 539Combined sources11
    Helixi541 – 547Combined sources7
    Beta strandi552 – 561Combined sources10
    Helixi565 – 574Combined sources10
    Helixi591 – 597Combined sources7
    Beta strandi605 – 608Combined sources4
    Helixi609 – 611Combined sources3
    Beta strandi615 – 619Combined sources5
    Turni623 – 625Combined sources3
    Helixi626 – 634Combined sources9
    Helixi635 – 640Combined sources6
    Turni642 – 644Combined sources3
    Beta strandi648 – 650Combined sources3
    Helixi653 – 655Combined sources3
    Helixi662 – 680Combined sources19
    Turni681 – 683Combined sources3
    Helixi685 – 687Combined sources3
    Turni690 – 693Combined sources4
    Helixi694 – 697Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2YR4X-ray1.70A/B2-714[»]
    2YR5X-ray1.25A/B2-714[»]
    2YR6X-ray1.35A/B2-714[»]
    3AYIX-ray1.25A/B2-714[»]
    3AYJX-ray1.10A/B2-714[»]
    3AYLX-ray1.25A/B2-714[»]
    ProteinModelPortaliQ5W9R9.
    SMRiQ5W9R9.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5W9R9.

    Family & Domainsi

    Sequence similaritiesi

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q5W9R9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGVTVIPRLL GLKDEKKIAT TVGEARLSGI NYRHPDSALV SYPVAAAAPL
    60 70 80 90 100
    GRLPAGNYRI AIVGGGAGGI AALYELGRLA ATLPAGSGID VQIYEADPDS
    110 120 130 140 150
    FLHDRPGIKA IKVRGLKAGR VSAALVHNGD PASGDTIYEV GAMRFPEIAG
    160 170 180 190 200
    LTWHYASAAF GDAAPIKVFP NPGKVPTEFV FGNRVDRYVG SDPKDWEDPD
    210 220 230 240 250
    SPTLKVLGVV AGGLVGNPQG ENVAMYPIAN VDPAKIAAIL NAATPPADAL
    260 270 280 290 300
    ERIQTKYWPE FIAQYDGLTL GAAVREIVTV AFEKGTLPPV DGVLDVDESI
    310 320 330 340 350
    SYYVELFGRF GFGTGGFKPL YNISLVEMMR LILWDYSNEY TLPVTENVEF
    360 370 380 390 400
    IRNLFLKAQN VGAGKLVVQV RQERVANACH SGTASARAQL LSYDSHNAVH
    410 420 430 440 450
    SEAYDFVILA VPHDQLTPIV SRSGFEHAAS QNLGDAGLGL ETHTYNQVYP
    460 470 480 490 500
    PLLLSDSSPA ANARIVTAIG QLHMARSSKV FATVKTAALD QPWVPQWRGE
    510 520 530 540 550
    PIKAVVSDSG LAASYVVPSP IVEDGQAPEY SSLLASYTWE DDSTRLRHDF
    560 570 580 590 600
    GLYPQNPATE TGTADGMYRT MVNRAYRYVK YAGASNAQPW WFYQLLAEAR
    610 620 630 640 650
    TADRFVFDWT TNKTAGGFKL DMTGDHHQSN LCFRYHTHAL AASLDNRFFI
    660 670 680 690 700
    ASDSYSHLGG WLEGAFMSAL NAVAGLIVRA NRGDVSALST EARPLVIGLR
    710
    PVVKVPAAEL ATSQ
    Length:714
    Mass (Da):76,883
    Last modified:December 7, 2004 - v1
    Checksum:i2EBEA742F1D41189
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti178E → W AA sequence (PubMed:9603998).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB167410 Genomic DNA. Translation: BAD66877.1.
    PIRiS41662.

    Genome annotation databases

    KEGGiag:BAD66877.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB167410 Genomic DNA. Translation: BAD66877.1.
    PIRiS41662.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2YR4X-ray1.70A/B2-714[»]
    2YR5X-ray1.25A/B2-714[»]
    2YR6X-ray1.35A/B2-714[»]
    3AYIX-ray1.25A/B2-714[»]
    3AYJX-ray1.10A/B2-714[»]
    3AYLX-ray1.25A/B2-714[»]
    ProteinModelPortaliQ5W9R9.
    SMRiQ5W9R9.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:BAD66877.

    Enzyme and pathway databases

    BRENDAi1.13.12.9. 5085.

    Miscellaneous databases

    EvolutionaryTraceiQ5W9R9.

    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 nameiPAO_PSESP
    AccessioniPrimary (citable) accession number: Q5W9R9
    Secondary accession number(s): Q7M1A6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 16, 2013
    Last sequence update: December 7, 2004
    Last modified: November 30, 2016
    This is version 50 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, Direct protein sequencing

    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.