PAMO_THEFY
ID PAMO_THEFY Reviewed; 542 AA.
AC Q47PU3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Phenylacetone monooxygenase;
DE Short=PAMO;
DE EC=1.14.13.92;
DE AltName: Full=Baeyer-Villiger monooxygenase;
DE Short=BVMO;
GN Name=pamO; OrderedLocusNames=Tfu_1490;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15599520; DOI=10.1007/s00253-004-1749-5;
RA Fraaije M.W., Wu J., Heuts D.P.H.M., van Hellemond E.W.,
RA Lutje Spelberg J.H., Janssen D.B.;
RT "Discovery of a thermostable Baeyer-Villiger monooxygenase by genome
RT mining.";
RL Appl. Microbiol. Biotechnol. 66:393-400(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FAD.
RX PubMed=15328411; DOI=10.1073/pnas.0404538101;
RA Malito E., Alfieri A., Fraaije M.W., Mattevi A.;
RT "Crystal structure of a Baeyer-Villiger monooxygenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13157-13162(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FAD AND NADP.
RX PubMed=21697090; DOI=10.1074/jbc.m111.255075;
RA Orru R., Dudek H.M., Martinoli C., Torres Pazmino D.E., Royant A., Weik M.,
RA Fraaije M.W., Mattevi A.;
RT "Snapshots of enzymatic Baeyer-Villiger catalysis: oxygen activation and
RT intermediate stabilization.";
RL J. Biol. Chem. 286:29284-29291(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH FAD.
RX PubMed=24443704; DOI=10.1021/cs400837z;
RA Martinoli C., Dudek H.M., Orru R., Edmondson D.E., Fraaije M.W.,
RA Mattevi A.;
RT "Beyond the protein matrix: Probing cofactor variants in a Baeyer-Villiger
RT oxygenation reaction.";
RL ACS Catal. 3:3058-3062(2013).
CC -!- FUNCTION: Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the
CC insertion of an oxygen atom into a carbon-carbon bond adjacent to a
CC carbonyl, which converts ketones to esters. Is most efficient with
CC phenylacetone as substrate, leading to the formation of benzyl acetate.
CC Can also oxidize other aromatic ketones (benzylacetone, alpha-
CC methylphenylacetone and 4-hydroxyacetophenone), some aliphatic ketones
CC (dodecan-2-one and bicyclohept-2-en-6-one) and sulfides (e.g. methyl 4-
CC tolylsulfide). {ECO:0000269|PubMed:15599520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADPH + O2 + phenylacetone = benzyl acetate + H2O +
CC NADP(+); Xref=Rhea:RHEA:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:52051, ChEBI:CHEBI:52052,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.92;
CC Evidence={ECO:0000269|PubMed:15599520};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:15599520};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:15599520};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for NADPH {ECO:0000269|PubMed:15599520};
CC KM=59 uM for phenylacetone {ECO:0000269|PubMed:15599520};
CC KM=360 uM for benzylacetone {ECO:0000269|PubMed:15599520};
CC KM=830 uM for alpha-methylphenylacetone
CC {ECO:0000269|PubMed:15599520};
CC KM=2.2 mM for 4-hydroxyacetophenone {ECO:0000269|PubMed:15599520};
CC KM=260 uM for 2-dodecanone {ECO:0000269|PubMed:15599520};
CC KM=15 mM for bicyclohept-2-en-6-one {ECO:0000269|PubMed:15599520};
CC KM=860 uM for methyl 4-tolylsulfide {ECO:0000269|PubMed:15599520};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15599520};
CC Temperature dependence:
CC Thermostable. Displays an activity half-life of 1 day at 52 degrees
CC Celsius. {ECO:0000269|PubMed:15599520};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15328411,
CC ECO:0000269|PubMed:15599520}.
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; CP000088; AAZ55526.1; -; Genomic_DNA.
DR RefSeq; WP_011291921.1; NC_007333.1.
DR PDB; 1W4X; X-ray; 1.70 A; A=1-542.
DR PDB; 2YLR; X-ray; 2.26 A; A=1-542.
DR PDB; 2YLS; X-ray; 2.26 A; A=1-542.
DR PDB; 2YLT; X-ray; 2.65 A; A=1-542.
DR PDB; 2YLW; X-ray; 2.90 A; A=1-542.
DR PDB; 2YLX; X-ray; 2.20 A; A=1-542.
DR PDB; 2YLZ; X-ray; 2.00 A; A=1-542.
DR PDB; 2YM1; X-ray; 2.28 A; A=1-542.
DR PDB; 2YM2; X-ray; 2.70 A; A=1-542.
DR PDB; 4C74; X-ray; 1.97 A; A=1-542.
DR PDB; 4C77; X-ray; 2.70 A; A=1-542.
DR PDB; 4D03; X-ray; 1.81 A; A=1-542.
DR PDB; 4D04; X-ray; 1.75 A; A=1-542.
DR PDB; 4OVI; X-ray; 1.87 A; A=1-542.
DR PDBsum; 1W4X; -.
DR PDBsum; 2YLR; -.
DR PDBsum; 2YLS; -.
DR PDBsum; 2YLT; -.
DR PDBsum; 2YLW; -.
DR PDBsum; 2YLX; -.
DR PDBsum; 2YLZ; -.
DR PDBsum; 2YM1; -.
DR PDBsum; 2YM2; -.
DR PDBsum; 4C74; -.
DR PDBsum; 4C77; -.
DR PDBsum; 4D03; -.
DR PDBsum; 4D04; -.
DR PDBsum; 4OVI; -.
DR AlphaFoldDB; Q47PU3; -.
DR SMR; Q47PU3; -.
DR STRING; 269800.Tfu_1490; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR EnsemblBacteria; AAZ55526; AAZ55526; Tfu_1490.
DR KEGG; tfu:Tfu_1490; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_006937_8_1_11; -.
DR OMA; DNIPGKP; -.
DR OrthoDB; 630753at2; -.
DR BRENDA; 1.14.13.92; 6298.
DR EvolutionaryTrace; Q47PU3; -.
DR GO; GO:0033776; F:phenylacetone monooxygenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
FT CHAIN 1..542
FT /note="Phenylacetone monooxygenase"
FT /id="PRO_0000287885"
FT BINDING 27
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15328411,
FT ECO:0000269|PubMed:21697090, ECO:0000269|PubMed:24443704"
FT BINDING 46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15328411,
FT ECO:0000269|PubMed:21697090, ECO:0000269|PubMed:24443704"
FT BINDING 54..57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15328411,
FT ECO:0000269|PubMed:21697090, ECO:0000269|PubMed:24443704"
FT BINDING 64..66
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21697090"
FT BINDING 66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15328411,
FT ECO:0000269|PubMed:21697090, ECO:0000269|PubMed:24443704"
FT BINDING 72
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15328411,
FT ECO:0000269|PubMed:21697090, ECO:0000269|PubMed:24443704"
FT BINDING 119
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15328411,
FT ECO:0000269|PubMed:21697090, ECO:0000269|PubMed:24443704"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15328411,
FT ECO:0000269|PubMed:21697090, ECO:0000269|PubMed:24443704"
FT BINDING 194..200
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21697090"
FT BINDING 217..218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21697090"
FT BINDING 336..337
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21697090"
FT BINDING 446
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15328411,
FT ECO:0000269|PubMed:21697090, ECO:0000269|PubMed:24443704"
FT BINDING 501
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21697090"
FT SITE 337
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:15328411,
FT ECO:0000269|PubMed:21697090"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1W4X"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1W4X"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 196..208
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:1W4X"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:1W4X"
FT TURN 293..297
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 299..316
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:2YLX"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1W4X"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:1W4X"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:4D04"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:1W4X"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:1W4X"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 446..466
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 476..490
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:1W4X"
FT HELIX 521..533
FT /evidence="ECO:0007829|PDB:1W4X"
FT STRAND 539..542
FT /evidence="ECO:0007829|PDB:1W4X"
SQ SEQUENCE 542 AA; 61124 MW; B24DF347F3D23D02 CRC64;
MAGQTTVDSR RQPPEEVDVL VVGAGFSGLY ALYRLRELGR SVHVIETAGD VGGVWYWNRY
PGARCDIESI EYCYSFSEEV LQEWNWTERY ASQPEILRYI NFVADKFDLR SGITFHTTVT
AAAFDEATNT WTVDTNHGDR IRARYLIMAS GQLSVPQLPN FPGLKDFAGN LYHTGNWPHE
PVDFSGQRVG VIGTGSSGIQ VSPQIAKQAA ELFVFQRTPH FAVPARNAPL DPEFLADLKK
RYAEFREESR NTPGGTHRYQ GPKSALEVSD EELVETLERY WQEGGPDILA AYRDILRDRD
ANERVAEFIR NKIRNTVRDP EVAERLVPKG YPFGTKRLIL EIDYYEMFNR DNVHLVDTLS
APIETITPRG VRTSEREYEL DSLVLATGFD ALTGALFKID IRGVGNVALK EKWAAGPRTY
LGLSTAGFPN LFFIAGPGSP SALSNMLVSI EQHVEWVTDH IAYMFKNGLT RSEAVLEKED
EWVEHVNEIA DETLYPMTAS WYTGANVPGK PRVFMLYVGG FHRYRQICDE VAAKGYEGFV
LT
