BVMO_PSEPK
ID BVMO_PSEPK Reviewed; 508 AA.
AC Q88J44;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Baeyer-Villiger monooxygenase {ECO:0000303|PubMed:17530181};
DE Short=BVMO {ECO:0000303|PubMed:17530181};
DE EC=1.14.13.- {ECO:0000269|PubMed:17530181};
GN OrderedLocusNames=PP_2805 {ECO:0000312|EMBL:AAN68413.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=17530181; DOI=10.1007/s10529-007-9401-y;
RA Rehdorf J., Kirschner A., Bornscheuer U.T.;
RT "Cloning, expression and characterization of a Baeyer-Villiger
RT monooxygenase from Pseudomonas putida KT2440.";
RL Biotechnol. Lett. 29:1393-1398(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. Preferentially converts short-chain
CC aliphatic ketones like 2-decanone, 3-decanone and 4-decanone. Some
CC acyclic ketones are converted not only to the alkylacetates, but also
CC methyl- and ethylesters are obtained, indicating insertion of oxygen on
CC both sides of the keto group. {ECO:0000269|PubMed:17530181}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P9WNF9};
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AE015451; AAN68413.1; -; Genomic_DNA.
DR RefSeq; NP_744949.1; NC_002947.4.
DR RefSeq; WP_010953714.1; NC_002947.4.
DR AlphaFoldDB; Q88J44; -.
DR SMR; Q88J44; -.
DR STRING; 160488.PP_2805; -.
DR EnsemblBacteria; AAN68413; AAN68413; PP_2805.
DR KEGG; ppu:PP_2805; -.
DR PATRIC; fig|160488.4.peg.2975; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_032067_2_0_6; -.
DR OMA; YPVDTHF; -.
DR PhylomeDB; Q88J44; -.
DR BioCyc; MetaCyc:G1G01-2985-MON; -.
DR BioCyc; PPUT160488:G1G01-2985-MON; -.
DR Proteomes; UP000000556; 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; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..508
FT /note="Baeyer-Villiger monooxygenase"
FT /id="PRO_0000431625"
FT BINDING 22
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 51..54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 61..63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 63
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 111
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 192..198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 215..216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
SQ SEQUENCE 508 AA; 56990 MW; FDD0C70AA6025EF7 CRC64;
MSSHTALPVE PLDVLIMGAG VSGIGAAAYL RRNQPNKTFA ILESRERMGG TWDLFRYPGI
RSDSDLYTFG FDFKPWTKAK SLADAADILE YLSEAIDEHQ LAPFIQYQQK VISANWQSDK
GLWSVRVEDG RTAQIRTVEC RWLFSAGGYY RYDQGFSPRF EGSEQFKGQI IHPQHWPEDL
DYTGKRVVVI GSGATAVTLI PAMADKVASI TMLQRTPSYI INQPANDGVA AFLRKVLPAQ
TAYSLTRYKN AKITLAFWGF CQRFPKLSKK LLLWLTRKEL PKDYPVDVHF NPPYNPWDQR
LCSVPEGDLF KAISAGNADI VTDHIERFTE HGVLLKSGKM LKADIIVTAT GLNVQLFGGI
TLHKDGKPVV LSETLAYKGM MLSGVPNFAF AVGYTNSSWT LKVCLLCDHF CRLLGLMERE
GYNVCEPKAP EGVETRPLLD FGAGYVQRAL DSMPRQGPRE PWVMSMDYFR DVKLLRRGAV
TDKCLKFTAV PNAPLHADVQ LQQQGSRR
