BVMO2_STRCO
ID BVMO2_STRCO Reviewed; 519 AA.
AC Q9RKB5;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=SCO3172 {ECO:0000312|EMBL:CAB59668.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
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; AL939115; CAB59668.1; -; Genomic_DNA.
DR RefSeq; NP_627388.1; NC_003888.3.
DR RefSeq; WP_011028809.1; NZ_VNID01000013.1.
DR AlphaFoldDB; Q9RKB5; -.
DR SMR; Q9RKB5; -.
DR STRING; 100226.SCO3172; -.
DR GeneID; 1098606; -.
DR KEGG; sco:SCO3172; -.
DR PATRIC; fig|100226.15.peg.3232; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_006937_7_1_11; -.
DR InParanoid; Q9RKB5; -.
DR OMA; WNTGGCT; -.
DR PhylomeDB; Q9RKB5; -.
DR Proteomes; UP000001973; 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; -; 3.
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..519
FT /note="Baeyer-Villiger monooxygenase"
FT /id="PRO_0000431627"
FT REGION 499..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 49..52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 59..61
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 110
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 183..189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 206..207
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 292..293
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 399
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT SITE 293
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
SQ SEQUENCE 519 AA; 56673 MW; 4031FB54427A57B4 CRC64;
MAEHEQVHEH VRVAVIGSGF GGLGAAVRLR REGITDFVVL ERAGSVGGTW RDNSYPGCAC
DVPSHLYSFS FAPNPEWPRT FSGQEHIRAY LEHVADTFGL RPHLRFDSEV KRMAWDTEQL
RWEIETVRGT LTADVVVSAT GPLSDPKVPD IPGLDTFPGK VFHSARWDHD YDLAGQRVAM
IGTGASAIQI VPSIQPKVDR LTLFQRTPAW VMPRVDRAIS GAERALHRAL PATTKLRRGL
LWGIRELQVQ AFTKHPNELG FVEQIAKRNM GAAIKDPALR AKLTPDYRIG CKRILLSSTY
YPALAKPNVD VVASGLSEVR GSTLVAADGT EAEADAIVFG TGFHVTDMPI AERVVGADGR
TLAETWKGGM EALRGGTAAG FPNFMTVIGP NTGLGNSSMI LMIESQLNYL ADYLRQLNVL
GGRTALDPRP AAVRNWNHRV QERMKRTVWN TGGCTSWYLD ASGRNTTVWP GTTAEFRRET
RRVDLAEYQV LRPAPAQVGA KAAEADTGAD TGADAEVSA
