ID   BVMO_PSEBH              Reviewed;         545 AA.
AC   A3U3H1;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Baeyer-Villiger monooxygenase {ECO:0000303|PubMed:24903773};
DE            Short=BVMO {ECO:0000305};
DE            EC=1.14.13.- {ECO:0000269|PubMed:24903773};
GN   ORFNames=OB2597_18631;
OS   Pseudooceanicola batsensis (strain ATCC BAA-863 / DSM 15984 / KCTC 12145 /
OS   HTCC2597) (Oceanicola batsensis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Pseudooceanicola.
OX   NCBI_TaxID=252305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-863 / DSM 15984 / KCTC 12145 / HTCC2597;
RX   PubMed=20418400; DOI=10.1128/jb.00412-10;
RA   Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT   "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT   batsensis HTCC2597(TDelta).";
RL   J. Bacteriol. 192:3549-3550(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, AND
RP   BIOTECHNOLOGY.
RC   STRAIN=ATCC BAA-863 / DSM 15984 / KCTC 12145 / HTCC2597;
RX   PubMed=24903773; DOI=10.1039/c4cc02541e;
RA   Reignier T., de Berardinis V., Petit J.L., Mariage A., Hamze K.,
RA   Duquesne K., Alphand V.;
RT   "Broadening the scope of Baeyer-Villiger monooxygenase activities toward
RT   alpha,beta-unsaturated ketones: a promising route to chiral enol-lactones
RT   and ene-lactones.";
RL   Chem. Commun. (Camb.) 50:7793-7796(2014).
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 as
CC       an electron donor. Besides cycloalkanones, can use cyclic alpha,beta-
CC       unsaturated ketones as substrates, leading to conjugated ene-lactones.
CC       Can also act on methylated cycloalkanones and methylated cycloalkenones
CC       with high enantioselectivity in some cases.
CC       {ECO:0000269|PubMed:24903773}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:24903773};
CC   -!- BIOTECHNOLOGY: This enzyme offers a promising route for the synthesis
CC       of chiral ene-lactones, when expressed in an engineered strain deprived
CC       of enone reductase activity. {ECO:0000269|PubMed:24903773}.
CC   -!- MISCELLANEOUS: Displays a different regioselectivity from
CC       P.lavamentivorans BVMO.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AAMO01000015; EAQ01307.1; -; Genomic_DNA.
DR   RefSeq; WP_009804217.1; NZ_AAMO01000015.1.
DR   AlphaFoldDB; A3U3H1; -.
DR   SMR; A3U3H1; -.
DR   HOGENOM; CLU_006937_8_1_5; -.
DR   OrthoDB; 630753at2; -.
DR   Proteomes; UP000004318; Unassembled WGS sequence.
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   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..545
FT                   /note="Baeyer-Villiger monooxygenase"
FT                   /id="PRO_0000430340"
FT   BINDING         24
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   SITE            335
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   545 AA;  60558 MW;  367A6F12EE264483 CRC64;
     MNIQTENTKT VGADFDAVVI GAGFGGLYAV HKLRNEQGLN VRGYDSASDV GGTWWWNRYP
     GALSDTESYV YRYSFDKELL RKGRWKTRYL TQPEILEYMN EVADHLDLRR SYKFDTKVDG
     AHYNEKTGLW NVITDSGETV TAKYLVTGLG LLSATNVPKF KGIDDFKGRI LHTGAWPEGV
     DLSNKRVGII GTGSTGVQVI TATAPIAKHL TVFQRSAQYV VPIGNTPQDD ATIAEQKANY
     DNIWNQVKNS VVAFGFEESA EPAETASPEE RERVFEAAWQ RGGGFYFMFG TFCDIATSQV
     ANDAAADFIK GKIKQIVKDP KVAEKLTPKD LYAKRPLCGN NYYEVYNRDN VTLADVKADP
     IAEFTPNGIR LESGEEHELD IVIFATGFDA VDGNYVKMDL RGRGGVTMRD TWKEGPLGYL
     GMMEVDFPNF FMILGPNGPF TNLPPSIETQ VEWIADTICA MEEEGVQSVE PTVEARDAWV
     GTCREIADMT LFPKAESWIF GANIPGKKNA VMFYMAGIGN YRNAISAVKE EGYTSLIRDR
     TAEKV