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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei2 – 21FAD; via amide nitrogen1 Publication
    Binding sitei68 – 681FAD; via amide nitrogen1 Publication
    Binding sitei120 – 1201FAD1 Publication
    Binding sitei144 – 1441Substrate
    Binding sitei375 – 3751FAD; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei537 – 5371Substrate
    Binding sitei660 – 6601Substrate; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi95 – 962FAD1 Publication
    Nucleotide bindingi141 – 1444FAD1 Publication
    Nucleotide bindingi652 – 6532FAD1 Publication
    Nucleotide bindingi660 – 6623FAD1 Publication

    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 lineageiBacteriaProteobacteria

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi143 – 1431M → A: Reduces catalytic efficiency 10-fold. 1 Publication
    Mutagenesisi144 – 1441R → A: Abolishes catalytic activity. 1 Publication
    Mutagenesisi144 – 1441R → K: Reduces catalytic activity 400-fold. 1 Publication
    Mutagenesisi479 – 4791K → A: Reduces catalytic efficiency 200-fold. 1 Publication
    Mutagenesisi537 – 5371Y → A: Abolishes catalytic activity. 1 Publication
    Mutagenesisi537 – 5371Y → F: Reduces catalytic activity 17-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 1515Removed 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 PublicationPRO_0000424222Add
    BLAST
    Chaini16 – 10792Phenylalanine 2-monooxygenase alpha subunitPRO_5000051132Add
    BLAST
    Propeptidei108 – 1092Linker peptide1 PublicationPRO_0000424223
    Chaini110 – 714605Phenylalanine 2-monooxygenase beta subunitPRO_0000424224Add
    BLAST

    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

    1
    714
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 287Combined sources
    Turni29 – 313Combined sources
    Helixi35 – 373Combined sources
    Helixi42 – 454Combined sources
    Beta strandi55 – 639Combined sources
    Helixi67 – 8014Combined sources
    Beta strandi88 – 947Combined sources
    Helixi101 – 1033Combined sources
    Beta strandi121 – 1266Combined sources
    Helixi131 – 1333Combined sources
    Beta strandi135 – 1395Combined sources
    Helixi150 – 16011Combined sources
    Beta strandi177 – 1815Combined sources
    Beta strandi184 – 1918Combined sources
    Helixi193 – 1953Combined sources
    Beta strandi196 – 1983Combined sources
    Helixi202 – 21413Combined sources
    Beta strandi218 – 2214Combined sources
    Helixi233 – 2408Combined sources
    Helixi247 – 2559Combined sources
    Helixi257 – 2659Combined sources
    Helixi270 – 28314Combined sources
    Helixi290 – 2923Combined sources
    Helixi296 – 31015Combined sources
    Beta strandi312 – 3154Combined sources
    Helixi318 – 3203Combined sources
    Helixi325 – 3339Combined sources
    Turni334 – 3374Combined sources
    Beta strandi339 – 3413Combined sources
    Beta strandi343 – 3464Combined sources
    Helixi348 – 36114Combined sources
    Turni362 – 3643Combined sources
    Beta strandi365 – 3717Combined sources
    Beta strandi373 – 3808Combined sources
    Beta strandi382 – 3854Combined sources
    Beta strandi388 – 3947Combined sources
    Beta strandi399 – 40911Combined sources
    Helixi413 – 4208Combined sources
    Beta strandi421 – 4233Combined sources
    Beta strandi428 – 4347Combined sources
    Helixi436 – 4383Combined sources
    Beta strandi443 – 4497Combined sources
    Helixi459 – 47012Combined sources
    Beta strandi477 – 4859Combined sources
    Helixi486 – 4905Combined sources
    Beta strandi504 – 5074Combined sources
    Turni508 – 5114Combined sources
    Beta strandi512 – 5187Combined sources
    Beta strandi529 – 53911Combined sources
    Helixi541 – 5477Combined sources
    Beta strandi552 – 56110Combined sources
    Helixi565 – 57410Combined sources
    Helixi591 – 5977Combined sources
    Beta strandi605 – 6084Combined sources
    Helixi609 – 6113Combined sources
    Beta strandi615 – 6195Combined sources
    Turni623 – 6253Combined sources
    Helixi626 – 6349Combined sources
    Helixi635 – 6406Combined sources
    Turni642 – 6443Combined sources
    Beta strandi648 – 6503Combined sources
    Helixi653 – 6553Combined sources
    Helixi662 – 68019Combined sources
    Turni681 – 6833Combined sources
    Helixi685 – 6873Combined sources
    Turni690 – 6934Combined sources
    Helixi694 – 6974Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 17-708.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5W9R9.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.50.50.60. 3 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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti178 – 1781E → W AA sequence (PubMed:9603998).Curated

    Sequence databases

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

    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
    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. Positions 17-708.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi1.13.12.9. 5085.

    Miscellaneous databases

    EvolutionaryTraceiQ5W9R9.

    Family and domain databases

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

    Publicationsi

    1. "Sequencing and expression of the L-phenylalanine oxidase gene from Pseudomonas sp. P-501. Proteolytic activation of the proenzyme."
      Suzuki H., Higashi Y., Asano M., Suguro M., Kigawa M., Maeda M., Katayama S., Mukouyama E.B., Uchiyama K.
      J. Biochem. 136:617-627(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, PROTEOLYTIC PROCESSING.
      Strain: P-501.
    2. "New subunit in L-phenylalanine oxidase from Pseudomonas sp. P-501 and the primary structure."
      Mukouyama E.B., Suzuki H., Koyama H.
      Arch. Biochem. Biophys. 308:400-406(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 16-107, SUBUNIT.
      Strain: P-501.
    3. "Chemical modification of L-phenylalanine oxidase from Pseudomonas sp. P-501 by phenylglyoxal. Identification of one essential arginyl residue."
      Mukouyama E.B., Hirose T., Suzuki H.
      J. Biochem. 123:1097-1103(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 110-183.
    4. "Purification and characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501."
      Koyama H.
      J. Biochem. 92:1235-1240(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
    5. "Further characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501."
      Koyama H.
      J. Biochem. 93:1313-1319(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Oxidation and oxygenation of L-amino acids catalyzed by a L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501."
      Koyama H.
      J. Biochem. 96:421-427(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating)."
      Koyama H., Suzuki H.
      J. Biochem. 100:859-866(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    8. "Kinetic isotope effect of the L-phenylalanine oxidase from Pseudomonas sp. P-501."
      Ohta Y., Mukouyama E.B., Suzuki H.
      J. Biochem. 139:551-555(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    9. "Structural basis of proteolytic activation of L-phenylalanine oxidase from Pseudomonas sp. P-501."
      Ida K., Kurabayashi M., Suguro M., Hiruma Y., Hikima T., Yamomoto M., Suzuki H.
      J. Biol. Chem. 283:16584-16590(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-714 IN COMPLEX WITH FAD AND SUBSTRATE ANALOG, MUTAGENESIS OF MET-143 AND LYS-479.
      Strain: P-501.
    10. "High resolution X-ray crystal structures of L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. Structures of the enzyme-ligand complex and catalytic mechanism."
      Ida K., Suguro M., Suzuki H.
      J. Biochem. 150:659-669(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 2-714 IN COMPLEXES WITH L-PHENYLALANINE AND L-METHIONINE, MUTAGENESIS OF ARG-144 AND TYR-537.
      Strain: P-501.

    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 11, 2015
    This is version 47 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.