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Phenylalanine 2-monooxygenase precursor (proPAO) (EC 1.13.12.9) (L-phenylalanine oxidase (deaminating and decarboxylating)) (PAO) [Cleaved into: Phenylalanine 2-monooxygenase alpha subunit; Phenylalanine 2-monooxygenase beta subunit]

 PAO_PSESP               Reviewed;         714 AA.
Q5W9R9; Q7M1A6;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 1.
25-OCT-2017, entry version 54.
RecName: Full=Phenylalanine 2-monooxygenase precursor;
Short=proPAO;
EC=1.13.12.9;
AltName: Full=L-phenylalanine oxidase (deaminating and decarboxylating);
Short=PAO;
Contains:
RecName: Full=Phenylalanine 2-monooxygenase alpha subunit;
Contains:
RecName: Full=Phenylalanine 2-monooxygenase beta subunit;
Flags: Precursor;
Pseudomonas sp.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=306;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR, AND PROTEOLYTIC
PROCESSING.
STRAIN=P-501;
PubMed=15632301; DOI=10.1093/jb/mvh169;
Suzuki H., Higashi Y., Asano M., Suguro M., Kigawa M., Maeda M.,
Katayama S., Mukouyama E.B., Uchiyama K.;
"Sequencing and expression of the L-phenylalanine oxidase gene from
Pseudomonas sp. P-501. Proteolytic activation of the proenzyme.";
J. Biochem. 136:617-627(2004).
[2]
PROTEIN SEQUENCE OF 16-107, AND SUBUNIT.
STRAIN=P-501;
PubMed=8109968; DOI=10.1006/abbi.1994.1056;
Mukouyama E.B., Suzuki H., Koyama H.;
"New subunit in L-phenylalanine oxidase from Pseudomonas sp. P-501 and
the primary structure.";
Arch. Biochem. Biophys. 308:400-406(1994).
[3]
PROTEIN SEQUENCE OF 110-183.
PubMed=9603998; DOI=10.1093/oxfordjournals.jbchem.a022048;
Mukouyama E.B., Hirose T., Suzuki H.;
"Chemical modification of L-phenylalanine oxidase from Pseudomonas sp.
P-501 by phenylglyoxal. Identification of one essential arginyl
residue.";
J. Biochem. 123:1097-1103(1998).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
PubMed=7174643; DOI=10.1093/oxfordjournals.jbchem.a134041;
Koyama H.;
"Purification and characterization of a novel L-phenylalanine oxidase
(deaminating and decarboxylating) from Pseudomonas sp. P-501.";
J. Biochem. 92:1235-1240(1982).
[5]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=6885723; DOI=10.1093/oxfordjournals.jbchem.a134265;
Koyama H.;
"Further characterization of a novel L-phenylalanine oxidase
(deaminating and decarboxylating) from Pseudomonas sp. P-501.";
J. Biochem. 93:1313-1319(1983).
[6]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=6501250;
Koyama H.;
"Oxidation and oxygenation of L-amino acids catalyzed by a L-
phenylalanine oxidase (deaminating and decarboxylating) from
Pseudomonas sp. P-501.";
J. Biochem. 96:421-427(1984).
[7]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=3818566; DOI=10.1093/oxfordjournals.jbchem.a121798;
Koyama H., Suzuki H.;
"Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase
(deaminating and decarboxylating).";
J. Biochem. 100:859-866(1986).
[8]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=16567420; DOI=10.1093/jb/mvj049;
Ohta Y., Mukouyama E.B., Suzuki H.;
"Kinetic isotope effect of the L-phenylalanine oxidase from
Pseudomonas sp. P-501.";
J. Biochem. 139:551-555(2006).
[9]
X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 2-714 IN COMPLEX WITH FAD
AND SUBSTRATE ANALOG, AND MUTAGENESIS OF MET-143 AND LYS-479.
STRAIN=P-501;
PubMed=18417467; DOI=10.1074/jbc.M800366200;
Ida K., Kurabayashi M., Suguro M., Hiruma Y., Hikima T., Yamomoto M.,
Suzuki H.;
"Structural basis of proteolytic activation of L-phenylalanine oxidase
from Pseudomonas sp. P-501.";
J. Biol. Chem. 283:16584-16590(2008).
[10]
X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 2-714 IN COMPLEXES WITH
L-PHENYLALANINE AND L-METHIONINE, AND MUTAGENESIS OF ARG-144 AND
TYR-537.
STRAIN=P-501;
PubMed=21841183; DOI=10.1093/jb/mvr103;
Ida K., Suguro M., Suzuki H.;
"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.";
J. Biochem. 150:659-669(2011).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:15632301, ECO:0000269|PubMed:16567420,
ECO:0000269|PubMed:3818566, ECO:0000269|PubMed:6501250,
ECO:0000269|PubMed:6885723, ECO:0000269|PubMed:7174643}.
-!- CATALYTIC ACTIVITY: L-phenylalanine + O(2) = 2-phenylacetamide +
CO(2) + H(2)O. {ECO:0000269|PubMed:16567420,
ECO:0000269|PubMed:6885723, ECO:0000269|PubMed:7174643}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:15632301,
ECO:0000269|PubMed:6885723};
Note=Binds 2 FAD per tetramer. {ECO:0000269|PubMed:15632301,
ECO:0000269|PubMed:6885723};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=11.1 uM for L-Phe (for the oxygenation reaction)
{ECO:0000269|PubMed:3818566, ECO:0000269|PubMed:6501250,
ECO:0000269|PubMed:6885723};
KM=13.3 uM for L-Phe (for the oxidation reaction)
{ECO:0000269|PubMed:3818566, ECO:0000269|PubMed:6501250,
ECO:0000269|PubMed:6885723};
KM=4 mM for L-Tyr {ECO:0000269|PubMed:3818566,
ECO:0000269|PubMed:6501250, ECO:0000269|PubMed:6885723};
KM=2.2 mM for L-Met {ECO:0000269|PubMed:3818566,
ECO:0000269|PubMed:6501250, ECO:0000269|PubMed:6885723};
KM=1.96 mM for O(2) (for the oxygenation reaction with L-Phe as
cosubstrate) {ECO:0000269|PubMed:3818566,
ECO:0000269|PubMed:6501250, ECO:0000269|PubMed:6885723};
KM=2.04 mM for O(2) (for the oxidation reaction with L-Phe as
cosubstrate) {ECO:0000269|PubMed:3818566,
ECO:0000269|PubMed:6501250, ECO:0000269|PubMed:6885723};
KM=3.145 mM for for O(2) (with L-Tyr as cosubstrate)
{ECO:0000269|PubMed:3818566, ECO:0000269|PubMed:6501250,
ECO:0000269|PubMed:6885723};
KM=1.258 mM for for O(2) (with L-Met as cosubstrate)
{ECO:0000269|PubMed:3818566, ECO:0000269|PubMed:6501250,
ECO:0000269|PubMed:6885723};
pH dependence:
Optimum pH is 6-9 for the oxygenation reaction and 10.5 for the
oxidation reaction. {ECO:0000269|PubMed:3818566,
ECO:0000269|PubMed:6501250, ECO:0000269|PubMed:6885723};
Temperature dependence:
Optimum temperature is 45 degrees Celsius for the oxygenation
reaction and 65 degrees Celsius for the oxygenation reaction.
Stable up to 70 degrees Celsius. {ECO:0000269|PubMed:3818566,
ECO:0000269|PubMed:6501250, ECO:0000269|PubMed:6885723};
-!- SUBUNIT: Heterotetramer composed of 2 alpha and 2 beta subunits.
{ECO:0000269|PubMed:18417467, ECO:0000269|PubMed:8109968}.
-!- PTM: 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. {ECO:0000269|PubMed:15632301}.
-!- SIMILARITY: Belongs to the phenylalanine 2-monooxygenase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB167410; BAD66877.1; -; Genomic_DNA.
PIR; S41662; S41662.
PDB; 2YR4; X-ray; 1.70 A; A/B=2-714.
PDB; 2YR5; X-ray; 1.25 A; A/B=2-714.
PDB; 2YR6; X-ray; 1.35 A; A/B=2-714.
PDB; 3AYI; X-ray; 1.25 A; A/B=2-714.
PDB; 3AYJ; X-ray; 1.10 A; A/B=2-714.
PDB; 3AYL; X-ray; 1.25 A; A/B=2-714.
PDBsum; 2YR4; -.
PDBsum; 2YR5; -.
PDBsum; 2YR6; -.
PDBsum; 3AYI; -.
PDBsum; 3AYJ; -.
PDBsum; 3AYL; -.
ProteinModelPortal; Q5W9R9; -.
SMR; Q5W9R9; -.
KEGG; ag:BAD66877; -.
KO; K21795; -.
BRENDA; 1.13.12.9; 5085.
EvolutionaryTrace; Q5W9R9; -.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0050172; F:phenylalanine 2-monooxygenase activity; IDA:UniProtKB.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
SUPFAM; SSF51905; SSF51905; 3.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; FAD; Flavoprotein;
Monooxygenase; Nucleotide-binding; Oxidoreductase; Zymogen.
PROPEP 1 15 Removed in mature form; occupies the
channel of the substrate amino acid from
the outside of the protein to the
interior flavin ring in the precursor.
{ECO:0000269|PubMed:8109968}.
/FTId=PRO_0000424222.
CHAIN 16 107 Phenylalanine 2-monooxygenase alpha
subunit.
/FTId=PRO_5000051132.
PROPEP 108 109 Linker peptide.
{ECO:0000269|PubMed:9603998}.
/FTId=PRO_0000424223.
CHAIN 110 714 Phenylalanine 2-monooxygenase beta
subunit.
/FTId=PRO_0000424224.
NP_BIND 95 96 FAD. {ECO:0000269|PubMed:18417467}.
NP_BIND 141 144 FAD. {ECO:0000269|PubMed:18417467}.
NP_BIND 652 653 FAD. {ECO:0000269|PubMed:18417467}.
NP_BIND 660 662 FAD. {ECO:0000269|PubMed:18417467}.
BINDING 2 2 FAD; via amide nitrogen.
{ECO:0000269|PubMed:18417467}.
BINDING 68 68 FAD; via amide nitrogen.
{ECO:0000269|PubMed:18417467}.
BINDING 120 120 FAD. {ECO:0000269|PubMed:18417467}.
BINDING 144 144 Substrate.
BINDING 375 375 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:18417467}.
BINDING 537 537 Substrate.
BINDING 660 660 Substrate; via carbonyl oxygen.
MUTAGEN 143 143 M->A: Reduces catalytic efficiency 10-
fold. {ECO:0000269|PubMed:18417467}.
MUTAGEN 144 144 R->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:21841183}.
MUTAGEN 144 144 R->K: Reduces catalytic activity 400-
fold. {ECO:0000269|PubMed:21841183}.
MUTAGEN 479 479 K->A: Reduces catalytic efficiency 200-
fold. {ECO:0000269|PubMed:18417467}.
MUTAGEN 537 537 Y->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:21841183}.
MUTAGEN 537 537 Y->F: Reduces catalytic activity 17-fold.
{ECO:0000269|PubMed:21841183}.
CONFLICT 178 178 E -> W (in Ref. 3; AA sequence).
{ECO:0000305}.
HELIX 22 28 {ECO:0000244|PDB:3AYJ}.
TURN 29 31 {ECO:0000244|PDB:2YR5}.
HELIX 35 37 {ECO:0000244|PDB:3AYJ}.
HELIX 42 45 {ECO:0000244|PDB:3AYJ}.
STRAND 55 63 {ECO:0000244|PDB:3AYJ}.
HELIX 67 80 {ECO:0000244|PDB:3AYJ}.
STRAND 88 94 {ECO:0000244|PDB:3AYJ}.
HELIX 101 103 {ECO:0000244|PDB:3AYJ}.
STRAND 121 126 {ECO:0000244|PDB:3AYJ}.
HELIX 131 133 {ECO:0000244|PDB:3AYJ}.
STRAND 135 139 {ECO:0000244|PDB:3AYJ}.
HELIX 150 160 {ECO:0000244|PDB:3AYJ}.
STRAND 177 181 {ECO:0000244|PDB:3AYJ}.
STRAND 184 191 {ECO:0000244|PDB:3AYJ}.
HELIX 193 195 {ECO:0000244|PDB:3AYJ}.
STRAND 196 198 {ECO:0000244|PDB:3AYJ}.
HELIX 202 214 {ECO:0000244|PDB:3AYJ}.
STRAND 218 221 {ECO:0000244|PDB:3AYJ}.
HELIX 233 240 {ECO:0000244|PDB:3AYJ}.
HELIX 247 255 {ECO:0000244|PDB:3AYJ}.
HELIX 257 265 {ECO:0000244|PDB:3AYJ}.
HELIX 270 283 {ECO:0000244|PDB:3AYJ}.
HELIX 290 292 {ECO:0000244|PDB:3AYJ}.
HELIX 296 310 {ECO:0000244|PDB:3AYJ}.
STRAND 312 315 {ECO:0000244|PDB:3AYJ}.
HELIX 318 320 {ECO:0000244|PDB:3AYJ}.
HELIX 325 333 {ECO:0000244|PDB:3AYJ}.
TURN 334 337 {ECO:0000244|PDB:3AYJ}.
STRAND 339 341 {ECO:0000244|PDB:2YR4}.
STRAND 343 346 {ECO:0000244|PDB:3AYJ}.
HELIX 348 361 {ECO:0000244|PDB:3AYJ}.
TURN 362 364 {ECO:0000244|PDB:3AYJ}.
STRAND 365 371 {ECO:0000244|PDB:3AYJ}.
STRAND 373 380 {ECO:0000244|PDB:3AYJ}.
STRAND 382 385 {ECO:0000244|PDB:3AYJ}.
STRAND 388 394 {ECO:0000244|PDB:3AYJ}.
STRAND 399 409 {ECO:0000244|PDB:3AYJ}.
HELIX 413 420 {ECO:0000244|PDB:3AYJ}.
STRAND 421 423 {ECO:0000244|PDB:3AYJ}.
STRAND 428 434 {ECO:0000244|PDB:3AYJ}.
HELIX 436 438 {ECO:0000244|PDB:3AYJ}.
STRAND 443 449 {ECO:0000244|PDB:3AYJ}.
HELIX 459 470 {ECO:0000244|PDB:3AYJ}.
STRAND 477 485 {ECO:0000244|PDB:3AYJ}.
HELIX 486 490 {ECO:0000244|PDB:3AYJ}.
STRAND 504 507 {ECO:0000244|PDB:3AYJ}.
TURN 508 511 {ECO:0000244|PDB:3AYJ}.
STRAND 512 518 {ECO:0000244|PDB:3AYJ}.
STRAND 529 539 {ECO:0000244|PDB:3AYJ}.
HELIX 541 547 {ECO:0000244|PDB:3AYJ}.
STRAND 552 561 {ECO:0000244|PDB:3AYJ}.
HELIX 565 574 {ECO:0000244|PDB:3AYJ}.
HELIX 591 597 {ECO:0000244|PDB:3AYJ}.
STRAND 605 608 {ECO:0000244|PDB:3AYJ}.
HELIX 609 611 {ECO:0000244|PDB:3AYJ}.
STRAND 615 619 {ECO:0000244|PDB:3AYJ}.
TURN 623 625 {ECO:0000244|PDB:3AYJ}.
HELIX 626 634 {ECO:0000244|PDB:3AYJ}.
HELIX 635 640 {ECO:0000244|PDB:3AYJ}.
TURN 642 644 {ECO:0000244|PDB:3AYJ}.
STRAND 648 650 {ECO:0000244|PDB:3AYJ}.
HELIX 653 655 {ECO:0000244|PDB:3AYJ}.
HELIX 662 680 {ECO:0000244|PDB:3AYJ}.
TURN 681 683 {ECO:0000244|PDB:3AYJ}.
HELIX 685 687 {ECO:0000244|PDB:3AYJ}.
TURN 690 693 {ECO:0000244|PDB:3AYJ}.
HELIX 694 697 {ECO:0000244|PDB:3AYJ}.
SEQUENCE 714 AA; 76883 MW; 2EBEA742F1D41189 CRC64;
MGVTVIPRLL GLKDEKKIAT TVGEARLSGI NYRHPDSALV SYPVAAAAPL GRLPAGNYRI
AIVGGGAGGI AALYELGRLA ATLPAGSGID VQIYEADPDS FLHDRPGIKA IKVRGLKAGR
VSAALVHNGD PASGDTIYEV GAMRFPEIAG LTWHYASAAF GDAAPIKVFP NPGKVPTEFV
FGNRVDRYVG SDPKDWEDPD SPTLKVLGVV AGGLVGNPQG ENVAMYPIAN VDPAKIAAIL
NAATPPADAL ERIQTKYWPE FIAQYDGLTL GAAVREIVTV AFEKGTLPPV DGVLDVDESI
SYYVELFGRF GFGTGGFKPL YNISLVEMMR LILWDYSNEY TLPVTENVEF IRNLFLKAQN
VGAGKLVVQV RQERVANACH SGTASARAQL LSYDSHNAVH SEAYDFVILA VPHDQLTPIV
SRSGFEHAAS QNLGDAGLGL ETHTYNQVYP PLLLSDSSPA ANARIVTAIG QLHMARSSKV
FATVKTAALD QPWVPQWRGE PIKAVVSDSG LAASYVVPSP IVEDGQAPEY SSLLASYTWE
DDSTRLRHDF GLYPQNPATE TGTADGMYRT MVNRAYRYVK YAGASNAQPW WFYQLLAEAR
TADRFVFDWT TNKTAGGFKL DMTGDHHQSN LCFRYHTHAL AASLDNRFFI ASDSYSHLGG
WLEGAFMSAL NAVAGLIVRA NRGDVSALST EARPLVIGLR PVVKVPAAEL ATSQ


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