BVMO_PARL1
ID BVMO_PARL1 Reviewed; 544 AA.
AC A7HU16;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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 OrderedLocusNames=Plav_1781;
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, AND
RP BIOTECHNOLOGY.
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
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 enol-lactones. Can also
CC act on methylated cycloalkanones and methylated cycloalkenones with
CC high enantioselectivity in some cases. {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 enol-lactones, when expressed in an engineered strain
CC deprived of enone reductase activity. {ECO:0000269|PubMed:24903773}.
CC -!- MISCELLANEOUS: Displays a different regioselectivity from O.batsensis
CC BVMO.
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; CP000774; ABS63399.1; -; Genomic_DNA.
DR RefSeq; WP_012110692.1; NC_009719.1.
DR PDB; 6JDK; X-ray; 2.50 A; A/B=1-544.
DR PDBsum; 6JDK; -.
DR AlphaFoldDB; A7HU16; -.
DR SMR; A7HU16; -.
DR STRING; 402881.Plav_1781; -.
DR EnsemblBacteria; ABS63399; ABS63399; Plav_1781.
DR KEGG; pla:Plav_1781; -.
DR eggNOG; COG2072; Bacteria.
DR HOGENOM; CLU_006937_8_0_5; -.
DR OMA; QYARSGQ; -.
DR OrthoDB; 630753at2; -.
DR Proteomes; UP000006377; 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 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 3D-structure; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..544
FT /note="Baeyer-Villiger monooxygenase"
FT /id="PRO_0000430341"
FT BINDING 27
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT SITE 340
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:6JDK"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 93..107
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 196..208
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 242..249
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6JDK"
FT TURN 294..298
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 300..317
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 321..327
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:6JDK"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 395..399
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:6JDK"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 449..469
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 479..493
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:6JDK"
FT HELIX 523..535
FT /evidence="ECO:0007829|PDB:6JDK"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:6JDK"
SQ SEQUENCE 544 AA; 61784 MW; EE41A566405FAD97 CRC64;
MSSVQSSQTQ KNDDAEVFDA LIVGAGFNGI YQLHRLRQEG FKVRLFEAGA DMGGIWYWNC
YPGARVDSHI PIYEFSIEEL WRDWNWTERF PAWDELRRYF HYVDKKLDLS RDIRFGMRVS
AAEFDEARDQ WVIRTTDGTV VRARFFILCT GFASKPYIPN YKGLESFAGE SFHTGLWPQE
GASFTGKRVG VVGTGASGVQ VVQEASKDAA HLTVFQRTPI LALPMQQRKL DVETQQRMKA
DYPEIFRIRR ETFGGFDILR DERSALEVPP EERCALYEKL WQKGGFHYWI GGFSDILTNE
EANRTMYDFW RDKTRARIKN PALADKLAPM EPPHPFGVKR PSLEQWYYEA FNQDNVSLVD
VREMPIVEIV PEGVLTSDGL VELDMLVLAT GFDAVTGGLT QIDIHGTGGI TLKEKWTEGA
RTYLGFATSG FPNMLFLYGP QSPSGFCNGP TCAEMQGEWV VDCLKHMREN NKGRIEATAQ
AEEEWAQLLN SIAGMTLFPR ADSWYMGANI PGKPRQLLNF PGVPIYMDQC NTAAAKDYEG
FVLD
