25DK1_PSEPU
ID 25DK1_PSEPU Reviewed; 363 AA.
AC Q6STM1; M5B4L6;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=2,5-diketocamphane 1,2-monooxygenase 1 {ECO:0000303|PubMed:21906366, ECO:0000303|PubMed:3944058};
DE Short=2,5-DKCMO 1 {ECO:0000303|PubMed:21906366, ECO:0000303|PubMed:23524667};
DE Short=2,5-diketocamphane monooxygenase 1 {ECO:0000303|PubMed:23524667};
DE EC=1.14.14.108 {ECO:0000269|PubMed:3944058};
DE AltName: Full=2,5-diketocamphane 1,2-monooxygenase oxygenating component {ECO:0000303|PubMed:3944058, ECO:0000303|PubMed:8515237};
DE AltName: Full=2,5-diketocamphane 1,2-monooxygenase oxygenating subunit {ECO:0000303|PubMed:21906366};
DE AltName: Full=Camphor 1,2-monooxygenase;
DE AltName: Full=Type II Baeyer-Villiger monooxygenase {ECO:0000303|PubMed:21906366};
DE Short=Type II BVMO {ECO:0000303|PubMed:21906366};
GN Name=camP {ECO:0000303|Ref.1};
GN Synonyms=camE25-1 {ECO:0000303|PubMed:23524667,
GN ECO:0000312|EMBL:BAN13281.1};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid CAM.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 17453 / DSM 50198 / JCM 6157 / NCIMB 10007 / NRRL B-4067 /
RC Stanier 77 / Biotype A; PLASMID=CAM;
RA Tongyoo N., Ward J.M.;
RT "camP, 2,5-diketocamphane 1,2-monooxygenase homolog, and camQ, lactone
RT hydrolase, on the CAM plasmid of Pseudomonas putida NCIMB 10007.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 17453 / DSM 50198 / JCM 6157 / NCIMB 10007 / NRRL B-4067 /
RC Stanier 77 / Biotype A; PLASMID=CAM;
RX PubMed=22267661; DOI=10.1128/aem.07694-11;
RA Leisch H., Shi R., Grosse S., Morley K., Bergeron H., Cygler M., Iwaki H.,
RA Hasegawa Y., Lau P.C.K.;
RT "Cloning, Baeyer-Villiger biooxidations, and structures of the camphor
RT pathway 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-coenzyme A
RT monooxygenase of Pseudomonas putida ATCC 17453.";
RL Appl. Environ. Microbiol. 78:2200-2212(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BVMO ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC 17453 / DSM 50198 / JCM 6157 / NCIMB 10007 / NRRL B-4067 /
RC Stanier 77 / Biotype A; PLASMID=CAM;
RX PubMed=23524667; DOI=10.1128/aem.03958-12;
RA Iwaki H., Grosse S., Bergeron H., Leisch H., Morley K., Hasegawa Y.,
RA Lau P.C.K.;
RT "Camphor pathway redux: functional recombinant expression of 2,5- and 3,6-
RT diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their
RT cognate flavin reductase catalyzing Baeyer-Villiger reactions.";
RL Appl. Environ. Microbiol. 79:3282-3293(2013).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND PATHWAY.
RC STRAIN=ATCC 17453 / DSM 50198 / JCM 6157 / NCIMB 10007 / NRRL B-4067 /
RC Stanier 77 / Biotype A; PLASMID=CAM;
RX PubMed=3944058; DOI=10.1128/jb.165.2.489-497.1986;
RA Taylor D.G., Trudgill P.W.;
RT "Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from
RT Pseudomonas putida ATCC 17453.";
RL J. Bacteriol. 165:489-497(1986).
RN [5]
RP FUNCTION, BVMO ACTIVITY, SUBUNIT, INDUCTION, AND PATHWAY.
RC STRAIN=ATCC 17453 / DSM 50198 / JCM 6157 / NCIMB 10007 / NRRL B-4067 /
RC Stanier 77 / Biotype A; PLASMID=CAM;
RX PubMed=8515237; DOI=10.1099/00221287-139-4-797;
RA Jones K.H., Smith R.T., Trudgill P.W.;
RT "Diketocamphane enantiomer-specific 'Baeyer-Villiger' monooxygenases from
RT camphor-grown Pseudomonas putida ATCC 17453.";
RL J. Gen. Microbiol. 139:797-805(1993).
RN [6]
RP FUNCTION, BVMO ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 17453 / DSM 50198 / JCM 6157 / NCIMB 10007 / NRRL B-4067 /
RC Stanier 77 / Biotype A; PLASMID=CAM;
RX PubMed=21906366; DOI=10.1186/2191-0855-1-13;
RA Kadow M., Sass S., Schmidt M., Bornscheuer U.T.;
RT "Recombinant expression and purification of the 2,5-diketocamphane 1,2-
RT monooxygenase from the camphor metabolizing Pseudomonas putida strain NCIMB
RT 10007.";
RL AMB Express 1:13-13(2011).
CC -!- FUNCTION: Involved in the degradation and assimilation of (+)-camphor,
CC which allows P.putida strain NCIMB 10007 to grow on this enantiomer of
CC camphor as the sole carbon source (PubMed:3944058, PubMed:8515237).
CC Catalyzes the FMNH(2)-dependent lactonization of 2,5-diketocamphane via
CC a Baeyer-Villiger oxidation to produce the unstable lactone 5-oxo-1,2-
CC campholide with (R,R) configuration, that presumably undergoes
CC spontaneous hydrolysis to form 2-oxo-Delta(3)-4,5,5-
CC trimethylcyclopentenylacetate (PubMed:3944058). Is also able to convert
CC (+)-camphor and norcamphor to the corresponding lactone in vitro
CC (PubMed:8515237, PubMed:21906366, PubMed:23524667). Shows no conversion
CC of (-)-camphor, (+)-fenchone, (-)-fenchone, and (+)-nopinone
CC (PubMed:23524667). Acts only on bicyclic ketones; is not active towards
CC monocyclic ketones, aromatic ketones, the aliphatic 2-decanone, 1-
CC indanone and progesterone (PubMed:21906366).
CC {ECO:0000269|PubMed:21906366, ECO:0000269|PubMed:23524667,
CC ECO:0000269|PubMed:3944058, ECO:0000269|PubMed:8515237,
CC ECO:0000305|PubMed:3944058, ECO:0000305|PubMed:8515237}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,4R)-bornane-2,5-dione + FMNH2 + O2 = (1R,4R)-5-oxo-1,2-
CC campholide + FMN + H(+) + H2O; Xref=Rhea:RHEA:34415,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15392, ChEBI:CHEBI:18130, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.108;
CC Evidence={ECO:0000269|PubMed:3944058};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:23524667};
CC -!- PATHWAY: Terpene metabolism; (R)-camphor degradation.
CC {ECO:0000305|PubMed:3944058, ECO:0000305|PubMed:8515237}.
CC -!- SUBUNIT: Homodimer (PubMed:3944058, PubMed:8515237, PubMed:23524667).
CC Likely forms a loose transient complex with a P.putida flavin reductase
CC that provides the required FMNH(2) to the enzyme (PubMed:3944058,
CC PubMed:8515237, PubMed:23524667). {ECO:0000269|PubMed:23524667,
CC ECO:0000269|PubMed:3944058, ECO:0000269|PubMed:8515237}.
CC -!- INDUCTION: By both (-)-camphor and (+)-camphor enantiomers.
CC {ECO:0000269|PubMed:8515237}.
CC -!- SIMILARITY: Belongs to the bacterial luciferase oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AY450285; AAR21560.1; -; Genomic_DNA.
DR EMBL; AB771747; BAN13281.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6STM1; -.
DR SMR; Q6STM1; -.
DR PRIDE; Q6STM1; -.
DR KEGG; ag:AAR21560; -.
DR BioCyc; MetaCyc:MON-3524; -.
DR BRENDA; 1.14.14.108; 5092.
DR UniPathway; UPA00719; -.
DR GO; GO:0018684; F:2,5-diketocamphane 1,2-monooxygenase; IEA:UniProtKB-EC.
DR GO; GO:0019383; P:(+)-camphor catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.30; -; 1.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR Pfam; PF00296; Bac_luciferase; 1.
DR SUPFAM; SSF51679; SSF51679; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; Monooxygenase; Oxidoreductase; Plasmid.
FT CHAIN 1..363
FT /note="2,5-diketocamphane 1,2-monooxygenase 1"
FT /id="PRO_0000422221"
FT BINDING 74
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:D7UER1"
FT BINDING 186..194
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:D7UER1"
SQ SEQUENCE 363 AA; 40704 MW; F1789C0F7C83F00D CRC64;
MKCGFFHTPY NLPTRTARQM FDWSLKLAQV CDEAGFADFM IGEHSTLAWE NIPCPEIIIG
AAAPLTKNIR FAPMAHLLPY HNPATLAIQI GWLSQILEGR YFLGVAPGGH HTDAILHGFE
GIGPLQEQMF ESLELMEKIW AREPFMEKGK FFQAGFPGPD TMPEYDVEIA DNSPWGGRES
MEVAVTGLTK NSSSLKWAGE RNYSPISFFG GHEVMRSHYD TWAAAMQSKG FTPERSRFRV
TRDIFIADTD AEAKKRAKAS GLGKSWEHYL FPIYKKFNLF PGIIADAGLD IDPSQVDMDF
LAEHVWLCGS PETVKGKIER MMERSGGCGQ IVVCSHDNID NPEPYFESLQ RLASEVLPKV
RMG
