BVMO1_STRCO
ID BVMO1_STRCO Reviewed; 603 AA.
AC Q9RL17;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=SCO0300 {ECO:0000312|EMBL:CAB55657.1};
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:Q47PU3};
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AL939104; CAB55657.1; -; Genomic_DNA.
DR RefSeq; NP_624628.1; NC_003888.3.
DR RefSeq; WP_003978566.1; NZ_VNID01000014.1.
DR AlphaFoldDB; Q9RL17; -.
DR SMR; Q9RL17; -.
DR STRING; 100226.SCO0300; -.
DR PRIDE; Q9RL17; -.
DR GeneID; 1095724; -.
DR KEGG; sco:SCO0300; -.
DR PATRIC; fig|100226.15.peg.274; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_006937_8_2_11; -.
DR InParanoid; Q9RL17; -.
DR OMA; ALKPWYG; -.
DR PhylomeDB; Q9RL17; -.
DR Proteomes; UP000001973; Chromosome.
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; IPR023753; FAD/NAD-binding_dom.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 3.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..603
FT /note="Baeyer-Villiger monooxygenase"
FT /id="PRO_0000431626"
FT BINDING 94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 102..105
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 112..114
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 164
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 248..254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 271..272
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 386..387
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT SITE 387
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
SQ SEQUENCE 603 AA; 66397 MW; 8E95654D5766F544 CRC64;
MAHAQELTPE ALAGLRERYR RERERRVRPD GTRQYLGADA EFGFYAADPW AGESDVREPV
RDRVDVAVVG GGFGGVLAGA RLRQQGVARV RVVEKGGDFG GTWYWNRYPG IHCDIEAHVY
LPMLDETGYV PEWKYAPGEE IRRHAMRIAE TFDLYTDVLF STAVTSLSWD DTTGEWIVET
DRHDAFRATY VITATGVLSE LKLPGIPGIE RFKGHTFHTS RWDYAYTGGG PDGGLTGLAD
KRVGVVGTGA TGVQVIPKLA EDAGQLHVFQ RTPSSVDVRA NRRTTARDVG ADRAGWASER
RDNFLRVVSG EAVEEDLVAD RWTATAGLLE KLLPSFRRPD DLAAFEAAYE VADAARMNDI
RARVDDLVTD PATADRLKPW YRYACKRPTF SDLYLQAFNR DNVTLVDTAD THGIERMNER
GVVVGDTEYP LDCLVFATGF SVGVSGVHSG RLPVRGRGGV RLRDAWSARG PRTLHGLTSN
GFPNLIQLGG VQSASSVNHT HVLDEHAVHG AALVAAAEAK GAVVEPTREA EDAWIATLAE
HAPDHAWFHA ECTPGYYNAE GRGRPNGPTA YPHGAAAFHE LLRRWREESM DELLAPRARV
RAC
