ID   DMXR6_CRYX8             Reviewed;         446 AA.
AC   A0A4P8DJZ3;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   23-FEB-2022, entry version 6.
DE   RecName: Full=Baeyer-Villiger monooxygenase dmxR6 {ECO:0000303|PubMed:30996871};
DE            Short=BVMO dmxR6 {ECO:0000303|PubMed:30996871};
DE            EC=1.-.-.- {ECO:0000305|PubMed:30996871};
DE   AltName: Full=Dimeric xanthone biosynthesis cluster protein R6 {ECO:0000303|PubMed:30996871};
GN   Name=dmxR6 {ECO:0000303|PubMed:30996871};
OS   Cryptosporiopsis sp. (strain 8999).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Dermateaceae; Cryptosporiopsis; unclassified Cryptosporiopsis.
OX   NCBI_TaxID=2572248;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP   PATHWAY.
RC   STRAIN=8999;
RX   PubMed=30996871; DOI=10.1039/c8sc05126g;
RA   Greco C., de Mattos-Shipley K., Bailey A.M., Mulholland N.P., Vincent J.L.,
RA   Willis C.L., Cox R.J., Simpson T.J.;
RT   "Structure revision of cryptosporioptides and determination of the genetic
RT   basis for dimeric xanthone biosynthesis in fungi.";
RL   Chem. Sci. 10:2930-2939(2019).
CC   -!- FUNCTION: Baeyer-Villiger monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of the dimeric xanthones cryptosporioptides
CC       (PubMed:30996871). The pathway begins with the synthesis of
CC       atrochrysone thioester by the polyketide synthase dmx-nrPKS (Probable).
CC       The atrochrysone carboxyl ACP thioesterase dmxR1 then breaks the
CC       thioester bond and releases the atrochrysone carboxylic acid from dmx-
CC       nrPKS (Probable). Atrochrysone carboxylic acid is decarboxylated by the
CC       decarboxylase dmxR15, and oxidized by the anthrone oxygenase dmxR16 to
CC       yield emodin (Probable). Emodin is then reduced to emodin hydroquinone
CC       by the oxidoreductase dmxR7 (Probable). A-ring reduction by the short
CC       chain dehydrogenase dmxR18, dehydration by the scytalone dehydratase-
CC       like protein dmxR17 and probable spontaneous re-oxidation, results in
CC       overall deoxygenation to chrysophanol (PubMed:30996871). Baeyer-
CC       Villiger oxidation by the Baeyer-Villiger monooxygenase (BVMO) dmxR6
CC       then yields monodictylactone in equilibrium with monodictyphenone
CC       (PubMed:30996871). In the case of the cryptosporioptides biosynthesis,
CC       monodictylactone is reduced at C-12 to an alcohol (by the short chain
CC       dehydrogenases dmxR12 or dmxR8) and hydroxylated at C-5 by dmxR9,
CC       yielding the electron-rich aromatic which could eliminate H(2)O to form
CC       the ortho-quinonemethide, followed by tautomerisation to paraquinone
CC       and complete the formal reduction to produce the 10-methylgroup
CC       (Probable). Conjugate addition of C-4a-OH to the resulting paraquinone
CC       by the monooxygenase dmxR10 then gives cyclohexadienone, which is then
CC       reduced at C-5 by the short chain dehydrogenase dmxR3 to give the
CC       dihydroxanthone (Probable). The 6,7-epoxide in the cryptosporioptides
CC       could be introduced by the cytochrome P450 monooxygenase dmxL3
CC       (Probable). The highly reducing PKS dmxL2 manufactures butyrate, which
CC       is further carboxylated by dmxL1 to form ethylmalonate
CC       (PubMed:30996871). It is not yet clear whether the carboxylation occurs
CC       while the butyrate is attached to the ACP of dmxL2, but this unusual
CC       fungal metabolite could then be esterified to O-5 by the O-
CC       acetyltransferase dmxR13 (PubMed:30996871). Finally, dimerization
CC       performed by dmxR5 gives the observed dimers cryptosporioptides A, B
CC       and C as the final products of the pathway (PubMed:30996871).
CC       {ECO:0000269|PubMed:30996871, ECO:0000305|PubMed:30996871}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:30996871}.
CC   -!- DISRUPTION PHENOTYPE: Leads to the accumulation of chrysophanol.
CC       {ECO:0000269|PubMed:30996871}.
CC   -!- SIMILARITY: Belongs to the AflY oxidoreductase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MK182094; QCL09097.1; -; Genomic_DNA.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR025337; Questin_oxidase-like.
DR   PANTHER; PTHR35870; PTHR35870; 1.
DR   Pfam; PF14027; Questin_oxidase; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase.
FT   CHAIN           1..446
FT                   /note="Baeyer-Villiger monooxygenase dmxR6"
FT                   /id="PRO_0000453472"
SQ   SEQUENCE   446 AA;  50678 MW;  4370336B22466313 CRC64;
     MAASPISLDP SHVGIIKVAN IPSDSLTECN KLLMKNHEEY HMFFRDTAGH NHIVHSLLTI
     LSLGASPKQL QDRYDDGIPI QRPIPKIDHE LLEKLSDPEI LLKTIGEITQ YHTLLEFFKR
     EIAAKGWKEA IQEYVLARTK IADTILARMY EGAYHPIIHL GLGIEFQQPI IVAEALAQAA
     SHDNSNIGTL FHNAEAEAGI SYPSRIPKPM IELINEVRAN ETIRTAPRWT DFGNKMRDGV
     VGRAGEAMAS LAAQFRIRND EEELKRSTAE MISTCAFFAG ASQHEGRKKK IDFFYMHNVT
     SSLFFTVFIR QDWIKLEDRV RLVEWKARLD LAWYAVSGSA ALDAKWISDY SNPASDGMGW
     EDLFTAVNEE HDDGHAAKFI RALKNGEQEC SKYEQGEWAD YFPMKGDMWL KLARMCQDTT
     TNRPPDLKWV PFTGFDQPWK RPDLAN