36DKM_PSEPU
ID 36DKM_PSEPU Reviewed; 378 AA.
AC D7UER1; H6W8H7; M5B4M0;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=3,6-diketocamphane 1,6-monooxygenase {ECO:0000303|PubMed:22286514, ECO:0000303|PubMed:8515237};
DE Short=3,6-DKCMO {ECO:0000303|PubMed:22286514, ECO:0000303|PubMed:23524667};
DE Short=3,6-DKMO {ECO:0000303|PubMed:26527149};
DE Short=3,6-diketocamphane monooxygenase {ECO:0000303|PubMed:23524667};
DE EC=1.14.14.155 {ECO:0000269|PubMed:23524667};
DE AltName: Full=3,6-diketocamphane monooxygenase oxygenating constituent {ECO:0000303|PubMed:22286514};
DE AltName: Full=3,6-diketocamphane monooxygenase oxygenating subunit {ECO:0000303|PubMed:26527149};
DE AltName: Full=Camphor 1,6-monooxygenase;
DE AltName: Full=Type II Baeyer-Villiger monooxygenase {ECO:0000303|PubMed:26527149};
DE Short=Type II BVMO {ECO:0000303|PubMed:26527149};
GN Name=camE36 {ECO:0000303|PubMed:23524667, ECO:0000312|EMBL:BAN13301.1};
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], FUNCTION, BVMO ACTIVITY, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ATCC 17453 / DSM 50198 / JCM 6157 / NCIMB 10007 / NRRL B-4067 /
RC Stanier 77 / Biotype A; PLASMID=CAM;
RX PubMed=22286514; DOI=10.1007/s00253-011-3859-1;
RA Kadow M., Loschinski K., Sass S., Schmidt M., Bornscheuer U.T.;
RT "Completing the series of BVMOs involved in camphor metabolism of
RT Pseudomonas putida NCIMB 10007 by identification of the two missing genes,
RT their functional expression in E. coli, and biochemical characterization.";
RL Appl. Microbiol. Biotechnol. 96:419-429(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC 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).
RN [3]
RP FUNCTION, BVMO ACTIVITY, SUBUNIT, AND INDUCTION.
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 [4] {ECO:0007744|PDB:4UWM, ECO:0007744|PDB:5AEC}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF THE NATIVE ENZYME AND IN COMPLEX
RP WITH FMN, AND SUBUNIT.
RX PubMed=26527149; DOI=10.1107/s1399004715017939;
RA Isupov M.N., Schroder E., Gibson R.P., Beecher J., Donadio G., Saneei V.,
RA Dcunha S.A., McGhie E.J., Sayer C., Davenport C.F., Lau P.C., Hasegawa Y.,
RA Iwaki H., Kadow M., Balke K., Bornscheuer U.T., Bourenkov G.,
RA Littlechild J.A.;
RT "The oxygenating constituent of 3,6-diketocamphane monooxygenase from the
RT CAM plasmid of Pseudomonas putida: the first crystal structure of a type II
RT Baeyer-Villiger monooxygenase.";
RL Acta Crystallogr. D 71:2344-2353(2015).
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:8515237). Catalyzes the
CC FMNH(2)-dependent lactonization of 3,6-diketocamphane via a Baeyer-
CC Villiger oxidation to produce the unstable lactone 5-oxo-1,2-campholide
CC with (S,S) configuration, that presumably undergoes spontaneous
CC hydrolysis to form 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetate
CC (PubMed:23524667). Is also able to convert (-)-camphor to the
CC corresponding lactone in vitro (PubMed:23524667, PubMed:22286514,
CC PubMed:8515237). Shows no conversion of (+)-camphor, (+)-fenchone, (-)-
CC fenchone, and (+)-nopinone. Acts on other bicyclic ketones but very
CC poorly on a few 2- and 4-substituted monocyclic ketones
CC (PubMed:23524667). {ECO:0000269|PubMed:22286514,
CC ECO:0000269|PubMed:23524667, ECO:0000269|PubMed:8515237,
CC ECO:0000305|PubMed:8515237}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,4S)-bornane-2,5-dione + FMNH2 + O2 = (1S,4S)-5-oxo-1,2-
CC campholide + FMN + H(+) + H2O; Xref=Rhea:RHEA:56596,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:36776, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:66896; EC=1.14.14.155;
CC Evidence={ECO:0000269|PubMed:23524667};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:23524667};
CC -!- SUBUNIT: Homodimer (PubMed:26527149, PubMed:23524667, PubMed:8515237).
CC Likely forms a loose transient complex with a P.putida flavin reductase
CC that provides the required FMNH(2) to the enzyme (PubMed:23524667,
CC PubMed:8515237). {ECO:0000269|PubMed:23524667,
CC ECO:0000269|PubMed:26527149, ECO:0000269|PubMed:8515237}.
CC -!- INDUCTION: By (-)-camphor and, to a lesser extent, by (+)-camphor.
CC {ECO:0000269|PubMed:8515237}.
CC -!- SIMILARITY: Belongs to the bacterial luciferase oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; JQ034404; AEZ35247.1; -; Genomic_DNA.
DR EMBL; AB771747; BAN13301.1; -; Genomic_DNA.
DR PDB; 4UWM; X-ray; 1.90 A; A/B=1-378.
DR PDB; 5AEC; X-ray; 2.00 A; A/B=1-378.
DR PDBsum; 4UWM; -.
DR PDBsum; 5AEC; -.
DR AlphaFoldDB; D7UER1; -.
DR SMR; D7UER1; -.
DR KEGG; ag:BAN13301; -.
DR BRENDA; 1.14.14.155; 5092.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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 3D-structure; Flavoprotein; FMN; Monooxygenase; Oxidoreductase; Plasmid.
FT CHAIN 1..378
FT /note="3,6-diketocamphane 1,6-monooxygenase"
FT /id="PRO_0000422222"
FT BINDING 10
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:26527149,
FT ECO:0007744|PDB:4UWM"
FT BINDING 44
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:26527149,
FT ECO:0007744|PDB:4UWM"
FT BINDING 76
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:26527149,
FT ECO:0007744|PDB:4UWM"
FT BINDING 201..209
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:26527149,
FT ECO:0007744|PDB:4UWM"
FT CONFLICT 278
FT /note="G -> S (in Ref. 1; AEZ35247)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 19..35
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:4UWM"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:4UWM"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:5AEC"
FT HELIX 139..155
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:4UWM"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 324..338
FT /evidence="ECO:0007829|PDB:4UWM"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:4UWM"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:4UWM"
SQ SEQUENCE 378 AA; 42314 MW; 0906E89366935D8E CRC64;
MAMETGLIFH PYMRPGRSAR QTFDWGIKSA VQADSVGIDS MMISEHASQI WENIPNPELL
IAAAALQTKN IKFAPMAHLL PHQHPAKLAT MIGWLSQILE GRYFLGIGAG AYPQASYMHG
IRNAGQSNTA TGGEETKNLN DMVRESLFIM EKIWKREPFF HEGKYWDAGY PEELEGEEGD
EQHKLADFSP WGGKAPEIAV TGFSYNSPSM RLAGERNFKP VSIFSGLDAL KRHWEVYSEA
AIEAGHTPDR SRHAVSHTVF CADTDKEAKR LVMEGPIGYC FERYLIPIWR RFGMMDGYAK
DAGIDPVDAD LEFLVDNVFL VGSPDTVTEK INALFEATGG WGTLQVEAHD YYDDPAPWFQ
SLELISKEVA PKILLPKR
