PENG_PENTH
ID PENG_PENTH Reviewed; 434 AA.
AC A0A1B2CTB2;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Prenyltransferase penG {ECO:0000303|PubMed:25859931};
DE EC=2.5.1.- {ECO:0000269|PubMed:25859931};
DE AltName: Full=Penigequinolones biosynthesis cluster protein G {ECO:0000303|PubMed:25859931};
GN Name=penG {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, CATALYTIC ACTIVITY, AND
RP 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: Prenyltransferase; 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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:25859931}.
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:25859931}.
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:25859931}.
CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC {ECO:0000305}.
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DR EMBL; KX528209; ANY57885.1; -; Genomic_DNA.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd13929; PT-DMATS_CymD; 1.
DR InterPro; IPR033964; Aro_prenylTrfase.
DR InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR InterPro; IPR012148; DMATS-type_fun.
DR PANTHER; PTHR40627; PTHR40627; 1.
DR Pfam; PF11991; Trp_DMAT; 1.
DR PIRSF; PIRSF000509; Trp_DMAT; 1.
DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE 1: Evidence at protein level;
KW Transferase.
FT CHAIN 1..434
FT /note="Prenyltransferase penG"
FT /id="PRO_0000455361"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104..105
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 108
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ SEQUENCE 434 AA; 49615 MW; 6E8EEB1C83489A1B CRC64;
MTQDVVTVSS QTAGTIKESG THSNPDNKTT SPSTWKSLSK YACFDSEAER QWWNDSGALI
ARFLDIAKGD IHEQYQYLLF VREVVIPALG PYPPIRRCCI NITEIGIELS LNYQGPGKPV
FRVSLDPISE MSGTPMDPLN IDTVNDTVAR LASIGLKDFD RTLHYHFMSE FCMPEEKAKT
YQQDSREPMA WSQMILGFDF KDGNVVTKEY IWTRHAAHAS GLHPHAIIRR AISRVDDQMR
CSAAVNLVLE YMETFNADIP VPFFSWDLID PSESRLKLYG IAWQWSWAKV EEVCTLGGKL
QGPATDRSIG LLRKLWGILK LDEFTPSMAF TWNYEILPGQ THPNVRIYFA ICDRSDEEVA
QAVSQWFNLL GWHETARSYP ETLRYLQPNR DLKKTNTAHT WLSITVTEKG VYTSLYYHPL
GNGPDDHNIR KTWF
