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PENA_PENTH
ID   PENA_PENTH              Reviewed;         432 AA.
AC   A0A1B2CTB0;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Monooxygenase penA {ECO:0000303|PubMed:25859931};
DE            EC=1.-.-.- {ECO:0000269|PubMed:25859931};
DE   AltName: Full=Penigequinolone biosynthesis cluster protein A {ECO:0000303|PubMed:25859931};
GN   Name=penA {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: Monooxygenase; part of the gene cluster that mediates the
CC       biosynthesis of penigequinolones, potent insecticidal alkaloids that
CC       contain a highly modified 10-carbon prenyl group (PubMed:25859931). The
CC       first stage is catalyzed by the nonribosomal pepdide synthetase penN
CC       that condenses anthranilic acid and O-methyl-L-tyrosine to produce 4'-
CC       methoxycyclopeptin (By similarity). 4'-methoxycyclopeptin is then
CC       converted to 4'-methoxydehydrocyclopeptin by the ketoglutarate-
CC       dependent dioxygenase penM through dehydrogenation to form a double
CC       bond between C-alpha and C-beta of the O-methyltyrosine side chain (By
CC       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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family.
CC       {ECO:0000305}.
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DR   EMBL; KX528209; ANY57879.1; -; Genomic_DNA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 2.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..432
FT                   /note="Monooxygenase penA"
FT                   /id="PRO_0000455353"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   432 AA;  46898 MW;  DEF412CEA412CF3B CRC64;
     MTRTSEFKIA IIGAGPAGLT LASLLTASPH PFNFTVFELR QRPHPSEVNL PCGNLDLQEG
     LGLQAIQACG LYPQFLEIES DCTQQSKVLD KNGKVLFDHV TQGQPEISRN ALTQLLLSSV
     PVDRIRWNTK VLAVTAADHS SGQGTVVSQE TTASTSTSET FDLIVGADGA WSRVRAVIPS
     APQPVYSGVC YITLYLPRLT EEYHELDQLI GGGTLAICGD GKLLLAQRTV RGTARVCLFL
     HSKCQPAVQR ALQSSGHDDR VGPNSILDAN SLLSTLPTRP EDLRELLLTN DDYFASWSDD
     IKHLLMVTLK EQPADAEIVA HPMHMLPLAP YPHTHMRGIV MVGDAAHLMT PFAGKGVNVA
     MADSLSLAEQ LEYLAVGRSS TMSFQDALDE ALVGYEEVAH PRAKKAMKLT WHNLLLSYSD
     NGAEQIGNVL ES
 
 
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