ID   CPNB_COMS9              Reviewed;         550 AA.
AC   Q8GAW0;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   04-NOV-2008, entry version 30.
DE   RecName: Full=Cyclopentanone 1,2-monooxygenase;
DE            Short=CPMO;
DE            EC=1.14.13.16;
GN   Name=cpnB;
OS   Comamonas sp. (strain NCIMB 9872).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=213664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-41.
RX   MEDLINE=22293557; PubMed=12406764;
RA   Iwaki H., Hasegawa Y., Wang S., Kayser M.M., Lau P.C.K.;
RT   "Cloning and characterization of a gene cluster involved in
RT   cyclopentanol metabolism in Comamonas sp. strain NCIMB 9872 and
RT   biotransformations effected by Escherichia coli-expressed
RT   cyclopentanone 1,2-monooxygenase.";
RL   Appl. Environ. Microbiol. 68:5671-5684(2002).
RN   [2]
RP   ERRATUM.
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   PROTEIN SEQUENCE OF 2-30, AND CHARACTERIZATION.
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
RT   9872.";
RL   J. Mol. Catal., B Enzym. 1:127-134(1996).
CC   -!- CATALYTIC ACTIVITY: Cyclopentanone + NADPH + O(2) = 5-
CC       valerolactone + NADP(+) + H(2)O.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Alcohol metabolism; cyclopentanol degradation; 5-
CC       valerolactone from cyclopentanol: step 2/2.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
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DR   EMBL; AB073151; BAC22652.1; -; Genomic_DNA.
DR   EMBL; AB022102; BAC01269.1; -; Genomic_DNA.
DR   GO; GO:0047799; F:cyclopentanone monooxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   Pfam; PF01266; DAO; 1.
DR   PRINTS; PR00368; FADPNR.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Monooxygenase; NADP;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    550       Cyclopentanone 1,2-monooxygenase.
FT                                /FTId=PRO_0000186453.
FT   NP_BIND      31     32       FAD (By similarity).
FT   BINDING      51     51       FAD (By similarity).
FT   BINDING      60     60       FAD (By similarity).
FT   BINDING      71     71       FAD (By similarity).
FT   BINDING      77     77       FAD (By similarity).
FT   BINDING     123    123       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   SITE        344    344       Transition state stabilizer (Potential).
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
//