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PENC_PENTH
ID   PENC_PENTH              Reviewed;         398 AA.
AC   A0A1B2CTA7;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=O-methyltransferase penC {ECO:0000303|PubMed:25859931};
DE            EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01020};
DE   AltName: Full=Penigequinolones biosynthesis cluster protein A {ECO:0000303|PubMed:25859931};
GN   Name=penC {ECO:0000303|PubMed:25859931};
OS   Penicillium thymicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=293382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=IBT 5891 / CBS 111225;
RX   PubMed=25859931; DOI=10.1021/jacs.5b03022;
RA   Zou Y., Zhan Z., Li D., Tang M., Cacho R.A., Watanabe K., Tang Y.;
RT   "Tandem prenyltransferases catalyze isoprenoid elongation and complexity
RT   generation in biosynthesis of quinolone alkaloids.";
RL   J. Am. Chem. Soc. 137:4980-4983(2015).
RN   [2]
RP   FUNCTION.
RX   PubMed=28114276; DOI=10.1038/nchembio.2283;
RA   Zou Y., Garcia-Borras M., Tang M.C., Hirayama Y., Li D.H., Li L.,
RA   Watanabe K., Houk K.N., Tang Y.;
RT   "Enzyme-catalyzed cationic epoxide rearrangements in quinolone alkaloid
RT   biosynthesis.";
RL   Nat. Chem. Biol. 13:325-332(2017).
CC   -!- FUNCTION: O-methyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of penigequinolones, potent insecticidal alkaloids
CC       that contain a highly modified 10-carbon prenyl group
CC       (PubMed:25859931). The first stage is catalyzed by the nonribosomal
CC       pepdide synthetase penN that condenses anthranilic acid and O-methyl-L-
CC       tyrosine to produce 4'-methoxycyclopeptin (By similarity). 4'-
CC       methoxycyclopeptin is then converted to 4'-methoxydehydrocyclopeptin by
CC       the ketoglutarate-dependent dioxygenase penM through dehydrogenation to
CC       form a double bond between C-alpha and C-beta of the O-methyltyrosine
CC       side chain (By similarity). PenM also converts its first product
CC       methoxydehydrocyclopeptin to 4'-methoxycyclopenin (By similarity). The
CC       following conversion of 4'methoxycyclopenin into 4'-methoxyviridicatin
CC       is catalyzed by the cyclopenase penL (By similarity). 4'-
CC       methoxyviridicatin is the precursor of quinolone natural products, and
CC       is further converted to quinolinone B (Probable). The prenyltransferase
CC       penI then catalyzes the canonical Friedel-Crafts alkylation of
CC       quinolinone B with dimethylallyl cation to yield dimethylallyl
CC       quinolone, which is subjected to FAD-dependent dehydrogenation by the
CC       FAD-linked oxidoreductase penH to yield conjugated aryl diene
CC       (PubMed:25859931). The delta(3') double bond then serves as the site of
CC       the second alkylation with DMAPP catalyzed by the prenyltransferase
CC       penG to yield a carbenium ion intermediate, which can be attacked by
CC       H(2)O to yield a styrenyl quinolone containing a C3'-hydroxyprenyl
CC       chain, or undergo cyclization to yield yaequinolones J1 and J2
CC       (PubMed:25859931). The conversion of the styrenyl quinolone into the
CC       tetrahydrofuran-containing yaequinolone C is performed by the FAD-
CC       dependent monooxygenase penE and involves epoxidation of the terminal
CC       C7'-C8' olefin, followed by epoxide ring opening initiated by the C3'
CC       hydroxyl group (PubMed:25859931). The predicted cysteine hydrolase penJ
CC       acts as an epoxide hydrolase that enhances the rate of the 5-exo-tet
CC       cyclization step, increasing the yield of yaequinolone C
CC       (PubMed:25859931, PubMed:28114276). PenF catalyzes the cationic
CC       rearrangement of the epoxide formed by penE (before ring opening to
CC       produce yaequinolone C) into yaequinolone D (PubMed:28114276). Finally,
CC       the short-chain dehydrogenase/reductase (SDR)-like reductase penD,
CC       catalyzes both the dehydration of yaequinolone D and the reduction of
CC       the resulting oxonium to yield penigequinolone (PubMed:28114276).
CC       {ECO:0000250|UniProtKB:C8VJQ3, ECO:0000250|UniProtKB:Q5AR53,
CC       ECO:0000250|UniProtKB:Q5AR54, ECO:0000269|PubMed:25859931,
CC       ECO:0000269|PubMed:28114276, ECO:0000305|PubMed:25859931}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:25859931}.
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000305|PubMed:25859931}.
CC   -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:25859931}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-independent O-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; KX528209; ANY57881.1; -; Genomic_DNA.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016461; COMT-like.
DR   InterPro; IPR001077; O_MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00891; Methyltransf_2; 1.
DR   PIRSF; PIRSF005739; O-mtase; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51683; SAM_OMT_II; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..398
FT                   /note="O-methyltransferase penC"
FT                   /id="PRO_0000455356"
FT   ACT_SITE        305
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT   BINDING         263
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
SQ   SEQUENCE   398 AA;  43665 MW;  D39305C50593336C CRC64;
     MTVGSQVVHD EPTILIAKLH ALEPRLKDKN DHQARKECLR ISKALTSQVE EPDNVAVSLA
     FSPVIALSAR VAIDLNLFAL VVQHGPVASA SLAALSGAEE LLIIRIMRLM STAHLVEETA
     ARTWSATRIT KAMAREEIAA GHRFNSQVVV PAIQSAPDFF RENGYSCPTD TRKGLVQYAL
     KTEQTAFDYI ISNPSMLKDF NLFMGNAMGA RKFWLDWFPV QSKILDGADP EKALIVDVGG
     GRGHDLIAFH KQFPNAGRLV VEDLPAVLEP LGEFSAFIEQ VEHDFLSGEQ PVKGARAYLC
     HHIMHDWPDS YCLRILEGIA LAMTPGYSKL LLHEIIVPEQ GACDFQAQSD ITAMVCNGGM
     ERTKQQFHTL LKAAGLSVVQ IWESADEGGD GIVEAMKV
 
 
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