ID   DMR13_CRYX8             Reviewed;         458 AA.
AC   A0A4V1DXC4;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=O-acetyltransferase dmxR13 {ECO:0000303|PubMed:30996871};
DE            EC=2.3.1.- {ECO:0000305|PubMed:30996871};
DE   AltName: Full=Dimeric xanthone biosynthesis cluster protein R13 {ECO:0000303|PubMed:30996871};
GN   Name=dmxR13 {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: O-acetyltransferase; part of the gene cluster that mediates
CC       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: Abolished production of cryptosprioptide C and D,
CC       but retains the production of cryptosporioptide A, however, in smaller
CC       quantities. {ECO:0000269|PubMed:30996871}.
CC   -!- SIMILARITY: Belongs to the trichothecene 3-O-acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; MK182094; QCL09104.1; -; Genomic_DNA.
DR   SMR; A0A4V1DXC4; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..458
FT                   /note="O-acetyltransferase dmxR13"
FT                   /id="PRO_0000453514"
FT   REGION          211..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  50193 MW;  DFE22DDA54AFE454 CRC64;
     MGSAIDFDLD GHLDILGQQP LLQMYTQICF AFPVADSSSY SAITKTLADG LERLSASFPW
     VAGHIVNEDS GEGNTGVFKI KPLDKSPSLI VKDFRNDPSF PTMEAIKKAG FPFSMLNEDI
     IAPRKTLPVR SDTPEISPVL VVQADLITGG LLLVFAGQHN AMDMTGQGQV IHLFSKACRN
     EPFTSDELVS GNLDRRTLVP LLDDSYKQGH ELARQISQPR PPPSSDGPPP PKLDWTYILF
     SPTSLAELKS LAQKTITFPS SFISTDDTLS AFVWQAVARS RLPRFDASAK TTCARAVDVR
     SYLGVPSTYT GLLQNVTYDT FTLQKLVNEP LGSVASALRS GLDPKRPNDL GFSTRALVTV
     LSRTLDKNTF SFGGTVNPSL DFMVSSWAKL DSYELDFGLG LGKPEGVRRP QFQPLESLGF
     LMPKTQDGEI AFALCLMEED MKRLRADEEF TKYGVFVG