BVMO_PSEAE
ID BVMO_PSEAE Reviewed; 527 AA.
AC Q9I3H5;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Baeyer-Villiger monooxygenase {ECO:0000303|PubMed:18051317};
DE Short=BVMO {ECO:0000303|PubMed:18051317};
DE EC=1.14.13.- {ECO:0000269|PubMed:18051317};
GN OrderedLocusNames=PA1538 {ECO:0000312|EMBL:AAG04927.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=18051317;
RA Park J., Kim D., Kim S., Kim J., Bae K., Lee C.;
RT "The analysis and application of a recombinant monooxygenase library as a
RT biocatalyst for the Baeyer-Villiger reaction.";
RL J. Microbiol. Biotechnol. 17:1083-1089(2007).
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 or lactones using NADPH
CC and/or NADH as an electron donor. Thus, can convert bicyclo[3.2.0]hept-
CC 2-en-6-one into the oxidative lactone products 2-oxabicyclo[3.3.0]oct-
CC 6-en-3-one and 3-oxabicyclo[3.3.0]oct-6-en-2-one. Is also able to
CC catalyze the sulfoxidation of methyl phenyl sulfide (thioanisole).
CC {ECO:0000269|PubMed:18051317}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q93TJ5};
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG04927.1; -; Genomic_DNA.
DR PIR; A83453; A83453.
DR RefSeq; NP_250229.1; NC_002516.2.
DR RefSeq; WP_010895574.1; NZ_QZGE01000032.1.
DR AlphaFoldDB; Q9I3H5; -.
DR SMR; Q9I3H5; -.
DR STRING; 287.DR97_398; -.
DR PaxDb; Q9I3H5; -.
DR EnsemblBacteria; AAG04927; AAG04927; PA1538.
DR GeneID; 880860; -.
DR KEGG; pae:PA1538; -.
DR PATRIC; fig|208964.12.peg.1591; -.
DR PseudoCAP; PA1538; -.
DR HOGENOM; CLU_006937_7_1_6; -.
DR InParanoid; Q9I3H5; -.
DR OMA; WNTGGCT; -.
DR PhylomeDB; Q9I3H5; -.
DR BioCyc; PAER208964:G1FZ6-1566-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..527
FT /note="Baeyer-Villiger monooxygenase"
FT /id="PRO_0000431624"
FT BINDING 36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 64..67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 74..76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 76
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 199..205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 222..223
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 308..309
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 415
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT SITE 309
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
SQ SEQUENCE 527 AA; 59467 MW; 2EDBBA8D947BBF02 CRC64;
MYTPANNHNR SLAMSTQPTP AAARHCKVAI IGTGFSGLGM AIRLRQEGED DFLIFEKDAG
VGGTWRVNNY PGCACDVQSH VYSFSFEANP EWTRMFARQP EIRAYLEKCW EKYRLQEKTL
LNTEIGKLAW DERQSLWHLH DAQGNHYTAN AVVSGMGGLS TPAYPRLDGL ENFQGKVFHS
QQWDHDYDLK GKRVAVIGTG ASAIQFVPEI QPLVAALDLY QRTPPWILPK PDRAISETER
RRFRRFPLVQ KLWRGGLYSL LEGRVLGFTF APQVMKLVQR LAIRHIHKQI KDPELRRKVT
PDYTIGCKRI LMSHNYYPAL AAANSTVITE GIRAVTANGI VDGNGREREV DAIIFGTGFT
ANDPIPRGVV FGRDGRDLLD SWSKGPEAYK GTTTAGFPNL FFLMGPNTGL GHNSMVYMIE
SQIAYVLDAL KLMKRRELLS LEVKAPVQER YNEYLQRKLD RSVWSVGGCK SWYLHPVSGR
NCTLWPGFTW RFRALTRQFD ASAYHLTTTP LAALSNEARQ QAEGVPA
