ID   DMR11_CRYX8             Reviewed;         262 AA.
AC   A0A4P8DJU7;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   31-JUL-2019, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Dimeric xanthone biosynthesis cluster protein R11 {ECO:0000303|PubMed:30996871};
GN   Name=dmxR11 {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, AND 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: Part of the gene cluster that mediates the biosynthesis of
CC       the dimeric xanthones cryptosporioptides (PubMed:30996871). The pathway
CC       begins with the synthesis of atrochrysone thioester by the polyketide
CC       synthase dmx-nrPKS (Probable). The atrochrysone carboxyl ACP
CC       thioesterase dmxR1 then breaks the thioester bond and releases the
CC       atrochrysone carboxylic acid from dmx-nrPKS (Probable). Atrochrysone
CC       carboxylic acid is decarboxylated by the decarboxylase dmxR15, and
CC       oxidized by the anthrone oxygenase dmxR16 to yield emodin (Probable).
CC       Emodin is then reduced to emodin hydroquinone by the oxidoreductase
CC       dmxR7 (Probable). A-ring reduction by the short chain dehydrogenase
CC       dmxR18, dehydration by the scytalone dehydratase-like protein dmxR17
CC       and probable spontaneous re-oxidation, results in overall deoxygenation
CC       to chrysophanol (PubMed:30996871). Baeyer-Villiger oxidation by the
CC       Baeyer-Villiger monooxygenase (BVMO) dmxR6 then yields monodictylactone
CC       in equilibrium with monodictyphenone (PubMed:30996871). In the case of
CC       the cryptosporioptides biosynthesis, monodictylactone is reduced at C-
CC       12 to an alcohol (by the short chain dehydrogenases dmxR12 or dmxR8)
CC       and hydroxylated at C-5 by dmxR9, yielding the electron-rich aromatic
CC       which could eliminate H(2)O to form the ortho-quinonemethide, followed
CC       by tautomerisation to paraquinone and complete the formal reduction to
CC       produce the 10-methylgroup (Probable). Conjugate addition of C-4a-OH to
CC       the resulting paraquinone by the monooxygenase dmxR10 then gives
CC       cyclohexadienone, which is then reduced at C-5 by the short chain
CC       dehydrogenase dmxR3 to give the dihydroxanthone (Probable). The 6,7-
CC       epoxide in the cryptosporioptides could be introduced by the cytochrome
CC       P450 monooxygenase dmxL3 (Probable). The highly reducing PKS dmxL2
CC       manufactures butyrate, which is further carboxylated by dmxL1 to form
CC       ethylmalonate (PubMed:30996871). It is not yet clear whether the
CC       carboxylation occurs while the butyrate is attached to the ACP of
CC       dmxL2, but this unusual fungal metabolite could then be esterified to
CC       O-5 by the O-acetyltransferase dmxR13 (PubMed:30996871). Finally,
CC       dimerization performed by dmxR5 gives the observed dimers
CC       cryptosporioptides A, B and C as the final products of the pathway
CC       (PubMed:30996871). {ECO:0000269|PubMed:30996871,
CC       ECO:0000305|PubMed:30996871}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:30996871}.
CC   -!- DOMAIN: The hemerythrin-like domain might act as a cathion-binding
CC       domain since it binds iron in haemerythrin, but can bind other metals
CC       in related proteins, such as cadmium or magnesium. {ECO:0000305}.
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DR   EMBL; MK182094; QCL09102.1; -; Genomic_DNA.
DR   SMR; A0A4P8DJU7; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055072; P:iron ion homeostasis; IEA:UniProt.
DR   InterPro; IPR012312; Hemerythrin-like.
DR   Pfam; PF01814; Hemerythrin; 1.
PE   4: Predicted;
KW   Metal-binding.
FT   CHAIN           1..262
FT                   /note="Dimeric xanthone biosynthesis cluster protein R11"
FT                   /id="PRO_0000453513"
FT   REGION          69..160
FT                   /note="Hemerythrin-like"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   262 AA;  30015 MW;  86BA7C6E33B576DA CRC64;
     MSTTSVIPKH WVDKGPWPIM TTPQGEGQDT NSHYSVFLAT DMCHVHNLFI RAMNSVYLQC
     PYVTDQADIA DLLFYTKTLV ITIDAHHDSE EKYLFPELAA YTKNPKIMAV NQAQHAAFHG
     GLEKLGEYCT TTSPADYSSV TFRAMIDSFA PQLFKHLNDE IPTILALKQY PSEDLKTIWT
     KTEQHIDDVG SFDEMFPLAF GCMDKGFEAG QHKFPPAPFF MEYVVRYWFA RKHSGAWRFN
     PCDMRGNPRQ LLFIPTEEDQ KP