BVMO4_DIESD
ID BVMO4_DIESD Reviewed; 612 AA.
AC U5S003;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Baeyer-Villiger monooxygenase 4 {ECO:0000303|PubMed:24949258};
DE Short=BVMO4 {ECO:0000303|PubMed:24949258};
DE EC=1.14.13.- {ECO:0000269|PubMed:24949258};
OS Dietzia sp. (strain D5).
OC Bacteria; Actinobacteria; Corynebacteriales; Dietziaceae; Dietzia;
OC unclassified Dietzia.
OX NCBI_TaxID=1408143;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=D5;
RX PubMed=24949258; DOI=10.1186/s13568-014-0023-1;
RA Bisagni S., Hatti-Kaul R., Mamo G.;
RT "Cloning, expression and characterization of a versatile Baeyer-Villiger
RT monooxygenase from Dietzia sp. D5.";
RL AMB Express 4:23-23(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. Has a broad substrate scope and oxidizes different
CC compounds including substituted and unsubstituted alicyclic, bicyclic-,
CC aliphatic-ketones, ketones with an aromatic moiety, and sulfides. The
CC highest activities are measured for 2- and 3-methylcyclohexanone,
CC phenylacetone, bicyclo[3.2.0]hept-2-en-6-one and menthone. Cannot use
CC NADH instead of NADPH. Is not active on benzaldehyde.
CC {ECO:0000269|PubMed:24949258}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:24949258};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.829 mM for phenylacetone {ECO:0000269|PubMed:24949258};
CC KM=0.507 mM for 2-methylcyclohexanone {ECO:0000269|PubMed:24949258};
CC KM=0.011 mM for NADPH {ECO:0000269|PubMed:24949258};
CC Note=kcat is 0.634 sec(-1) with phenylacetone as substrate and 0.370
CC sec(-1) with 2-methylcyclohexanone as substrate.
CC {ECO:0000269|PubMed:24949258};
CC pH dependence:
CC Optimum pH is 7.5. Exhibits more than 50% of its optimal activity
CC between pH 6.5 and 9.0. Displays highest stability in a pH range of
CC 7.0-8.0. {ECO:0000269|PubMed:24949258};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius. At this temperature, its
CC half-life is about 20 hours. Retains about 50% and 20% of its initial
CC activity after 20 h and 48 h of incubation at 35 degrees Celsius,
CC respectively. {ECO:0000269|PubMed:24949258};
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; KF319017; AGY78320.1; -; Genomic_DNA.
DR AlphaFoldDB; U5S003; -.
DR SMR; U5S003; -.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
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; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
FT CHAIN 1..612
FT /note="Baeyer-Villiger monooxygenase 4"
FT /id="PRO_0000431623"
FT BINDING 99
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 107..110
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 117..119
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 119
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 253..259
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 276..277
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT BINDING 393..394
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
FT SITE 394
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q47PU3"
SQ SEQUENCE 612 AA; 68454 MW; 13F1E417C13C4B58 CRC64;
MPFTLPESKI AIDIDFDPDH LRQRFEADKQ ARERKDQLAQ FQGLDDVLEV DDSDPFSEPI
TREPVTEELD ALVLGGGFGG LTAGAYLTQN GVENFRLVEY GGDFGGTWYW NRYPGVQCDI
ESHIYMPLLE ETGYVPSQRY ADGSEIFEHA QRIGRHYGLY DRTYFQTRAT HARWDEQIQR
WEVTTDRGDR FVTRVLLRSN GALTKPQLPK VPGIGDFEGK IFHTSRWDYG YTGGSAAGDL
AHLRDKRVAV VGTGATGVQV VPYLAQDAKE LVVVQRTPSV VQPRNNRKTD PEWVASLTPG
WQYERHDNFN GIISGHEVEG NLVDDGWTHL FPELTGQHLV DVPVGELPEG DQALVAELAD
MNLLMSAHAR VDSIVTDPAT ADGLKPWFGY MCKRPCFNDE YLEAFNRPNV TLAASPAGID
GITSSGIVVA GTHYEVDCII FATGFETGSG PAGIYGYDVI GREGHSMQEY FSEGARTFHG
FFTHGFPNFV ELGMSQTAYY VNFVYMLDRK ARHAARLVRH LLDSGIGTFE PTAEAEADWV
AEVRRSNEPR EAYWGACTPG YYNGQGEVSK AVFRDVYNSS EIDFWNMIEA WWNSGRFEGL
VFEPARDAVP VA
