25DK2_PSEPU
ID 25DK2_PSEPU Reviewed; 363 AA.
AC M5AWY0;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=2,5-diketocamphane 1,2-monooxygenase 2 {ECO:0000305|PubMed:23524667};
DE Short=2,5-DKCMO 2 {ECO:0000303|PubMed:23524667};
DE Short=2,5-diketocamphane monooxygenase 2 {ECO:0000303|PubMed:23524667};
DE EC=1.14.14.108 {ECO:0000250|UniProtKB:Q6STM1};
DE AltName: Full=2,5-diketocamphane 1,2-monooxygenase oxygenating component {ECO:0000303|PubMed:23524667};
DE AltName: Full=2,5-diketocamphane 1,2-monooxygenase oxygenating subunit {ECO:0000303|PubMed:23524667};
DE AltName: Full=Camphor 1,2-monooxygenase;
DE AltName: Full=Type II Baeyer-Villiger monooxygenase {ECO:0000303|PubMed:23524667};
DE Short=Type II BVMO {ECO:0000303|PubMed:23524667};
GN Name=camE25-2 {ECO:0000303|PubMed:23524667, ECO:0000312|EMBL:BAN13304.1};
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;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BVMO ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, 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).
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. Catalyzes the FMNH(2)-dependent
CC lactonization of 2,5-diketocamphane via a Baeyer-Villiger oxidation to
CC produce the unstable lactone 5-oxo-1,2-campholide with (R,R)
CC configuration, that presumably undergoes spontaneous hydrolysis to form
CC 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetate (By similarity). Is
CC also able to convert (+)-camphor and norcamphor to the corresponding
CC lactone in vitro. Shows no conversion of (-)-camphor, (+)-fenchone,
CC (-)-fenchone, and (+)-nopinone. Acts on other bicyclic ketones and, to
CC a lesser extent, on some 2- and 4-substituted monocyclic ketones
CC (PubMed:23524667). {ECO:0000250|UniProtKB:Q6STM1,
CC ECO:0000269|PubMed:23524667}.
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:0000250|UniProtKB:Q6STM1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:23524667};
CC -!- PATHWAY: Terpene metabolism; (R)-camphor degradation.
CC {ECO:0000250|UniProtKB:Q6STM1}.
CC -!- SUBUNIT: Homodimer. Likely forms a loose transient complex with a
CC P.putida flavin reductase that provides the required FMNH(2) to the
CC enzyme. {ECO:0000269|PubMed:23524667}.
CC -!- SIMILARITY: Belongs to the bacterial luciferase oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AB771747; BAN13304.1; -; Genomic_DNA.
DR AlphaFoldDB; M5AWY0; -.
DR SMR; M5AWY0; -.
DR BRENDA; 1.14.14.108; 5092.
DR UniPathway; UPA00719; -.
DR GO; GO:0018684; F:2,5-diketocamphane 1,2-monooxygenase; IEA:RHEA.
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 2"
FT /id="PRO_0000444572"
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; 40576 MW; DB782C17E1A42BC1 CRC64;
MQAGFFHTPY NLPTRTARQM FDWSLKLAQV CDEAGFADFM IGEHSTLAWE NIPCPEIIIG
AAAPLTKNIR FAPMAHLLPY HNPASLAIQV GWLSQILEGR YFLGVAPGGH HTDAILHGFE
GIGPLQEQMF EALELMEKVW ARKPFMEKGK FFQAGFPGPD TMPEYDVEIA DNSPWGGREA
LEIAVTGLTK NSSSLKWAGE RNYSPISFFG GHEVMRSHYD TWAAAMQSKG FTPDTSRFRV
TREIFIADTD AEARKRAKAS GMAKTWEHYL FPIYKKFNLF PGIIADAGLD IDPSQIDMDF
LADHVWLCGS PETVKGKIEN MIERSGGCGQ IIVNSHDNID NPEPYFESLQ RLAQEVLPNV
KTS
