ID   CPMO_COMS9              Reviewed;         550 AA.
AC   Q8GAW0; Q937L5;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Cyclopentanone 1,2-monooxygenase;
DE            Short=CPMO;
DE            EC=1.14.13.16;
DE   AltName: Full=Baeyer-Villiger monooxygenase;
DE            Short=BVMO;
GN   Name=cpnB; Synonyms=cpmA;
OS   Comamonas sp. (strain NCIMB 9872).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas; unclassified Comamonas.
OX   NCBI_TaxID=213664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-41, FUNCTION,
RP   CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, DISRUPTION PHENOTYPE,
RP   AND PATHWAY.
RC   STRAIN=NCIMB 9872;
RX   PubMed=12406764; DOI=10.1128/aem.68.11.5671-5684.2002;
RA   Iwaki H., Hasegawa Y., Wang S., Kayser M.M., Lau P.C.K.;
RT   "Cloning and characterization of a gene cluster involved in cyclopentanol
RT   metabolism in Comamonas sp. strain NCIMB 9872 and biotransformations
RT   effected by Escherichia coli-expressed cyclopentanone 1,2-monooxygenase.";
RL   Appl. Environ. Microbiol. 68:5671-5684(2002).
RN   [2]
RP   ERRATUM OF PUBMED:12406764.
RA   Iwaki H., Hasegawa Y., Wang S., Kayser M.M., Lau P.C.K.;
RL   Appl. Environ. Microbiol. 69:2414-2414(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=NCIMB 9872;
RX   PubMed=12588297; DOI=10.1046/j.1462-2920.2003.00401.x;
RA   van Beilen J.B., Mourlane F., Seeger M.A., Kovac J., Li Z., Smits T.H.M.,
RA   Fritsche U., Witholt B.;
RT   "Cloning of Baeyer-Villiger monooxygenases from Comamonas, Xanthobacter and
RT   Rhodococcus via PCR with highly degenerate primers.";
RL   Environ. Microbiol. 5:174-182(2003).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-30, SUBUNIT, AND CHARACTERIZATION.
RC   STRAIN=NCIMB 9872;
RA   Bes M.T., Villa R., Roberts S.M., Wan P.W.H., Willetts A.;
RT   "Oxidative biotransformations by microorganisms: production of chiral
RT   synthons by cyclopentanone monooxygenase from Pseudomonas sp. NCIMB 9872.";
RL   J. Mol. Catal., B Enzym. 1:127-134(1996).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND COFACTOR.
RC   STRAIN=NCIMB 9872;
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. Converts cyclopentanone to 5-valerolactone, a step
CC       in the degradation pathway of cyclopentanol. Besides cycloalkanones,
CC       can also act on methylated and other alkylated cycloalkanones, and on
CC       methylated cycloalkenones, with high enantioselectivity in some cases.
CC       Cannot use NADH instead of NADPH. {ECO:0000269|PubMed:12406764,
CC       ECO:0000269|PubMed:12588297, ECO:0000269|PubMed:24903773}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclopentanone + H(+) + NADPH + O2 = 5-valerolactone + H2O +
CC         NADP(+); Xref=Rhea:RHEA:15737, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16486, ChEBI:CHEBI:16545,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.16;
CC         Evidence={ECO:0000269|PubMed:12406764, ECO:0000269|PubMed:24903773};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:12406764, ECO:0000269|PubMed:24903773};
CC   -!- PATHWAY: Alcohol metabolism; cyclopentanol degradation; 5-valerolactone
CC       from cyclopentanol: step 2/2. {ECO:0000269|PubMed:12406764}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.4}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not capable of growth
CC       on cyclopentanol or cyclopentanone as a sole carbon and energy source.
CC       {ECO:0000269|PubMed:12406764}.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB073151; BAC22652.1; -; Genomic_DNA.
DR   EMBL; AB022102; BAC01269.1; -; Genomic_DNA.
DR   EMBL; AJ418060; CAD10798.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GAW0; -.
DR   SMR; Q8GAW0; -.
DR   KEGG; ag:BAC22652; -.
DR   BRENDA; 1.14.13.16; 1588.
DR   SABIO-RK; Q8GAW0; -.
DR   UniPathway; UPA00764; UER00750.
DR   GO; GO:0047799; F:cyclopentanone monooxygenase activity; IEA:UniProtKB-EC.
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:0033022; P:cyclopentanol catabolic process; IEA:UniProtKB-UniPathway.
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   Direct protein sequencing; FAD; Flavoprotein; Monooxygenase; NADP;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12406764, ECO:0000269|Ref.4"
FT   CHAIN           2..550
FT                   /note="Cyclopentanone 1,2-monooxygenase"
FT                   /id="PRO_0000186453"
FT   BINDING         31..32
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
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         77
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   SITE            344
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   550 AA;  62111 MW;  8956EF95203F6173 CRC64;
     MTTMTTMTTE QLGMNNSVND KLDVLLIGAG FTGLYQLYHL RKLGYKVHLV DAGADIGGIW
     HWNCYPGARV DTHCQIYQYS IPELWQEFNW KELFPNWAQM REYFHFADKK LDLSKDISFN
     TRVQSAVFDE GTREWTVRSI GHQPIQARFV IANLGFGASP STPNVDGIET FKGQWYHTAL
     WPQEGVNMAG KRVAIIGTGS SGVQVAQEAA LDAKQVTVYQ RTPNLALPMH QKQLSAEDNL
     RMKPELPAAF ERRGKCFAGF DFDFIAKNAT ELSAAERTEI LEELWNAGGF RYWLANFQDY
     LFDDKANDYV YEFWRDKVRA RIKDPKVAEK LAPMKKPHPY GAKRPSLEQW YYEIFNQNNV
     TLVDVNETPV LRITEKGIVT AEGEAEFDLI VFATGFDAVT GGLTSIDFRN NQGQSFKDVW
     SDGIRTQLGV ATAGFPNLLF GYGPQSPAGF CNGPSSAEYQ GDLLIQLMNY LRDNNISRIE
     AQSEAQEEWS KLIADFWDSS LFPRAKSWYQ GSNIPGKKVE SLNFPLGLPT YISKFNESAE
     KGYAGFSLAS