ID   VRTC_PENAE              Reviewed;         483 AA.
AC   D7PHZ4;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Prenyltransferase vrtC {ECO:0000303|PubMed:20534346};
DE            EC=2.5.1.- {ECO:0000305|PubMed:20534346};
DE   AltName: Full=Viridicatumtoxin synthesis protein C {ECO:0000303|PubMed:20534346};
GN   Name=vrtC {ECO:0000303|PubMed:20534346};
OS   Penicillium aethiopicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=IBT 5753;
RX   PubMed=20534346; DOI=10.1016/j.chembiol.2010.03.015;
RA   Chooi Y.H., Cacho R., Tang Y.;
RT   "Identification of the viridicatumtoxin and griseofulvin gene clusters from
RT   Penicillium aethiopicum.";
RL   Chem. Biol. 17:483-494(2010).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=19168978; DOI=10.1038/ja.2008.84;
RA   Zheng C.J., Yu H.E., Kim E.H., Kim W.G.;
RT   "Viridicatumtoxin B, a new anti-MRSA agent from Penicillium sp. FR11.";
RL   J. Antibiot. 61:633-637(2008).
RN   [3]
RP   FUNCTION.
RX   PubMed=24161266; DOI=10.1021/ja408966t;
RA   Chooi Y.H., Hong Y.J., Cacho R.A., Tantillo D.J., Tang Y.;
RT   "A cytochrome P450 serves as an unexpected terpene cyclase during fungal
RT   meroterpenoid biosynthesis.";
RL   J. Am. Chem. Soc. 135:16805-16808(2013).
RN   [4]
RP   BIOTECHNOLOGY.
RX   PubMed=27049441; DOI=10.1038/ja.2016.35;
RA   Inokoshi J., Nakamura Y., Komada S., Komatsu K., Umeyama H., Tomoda H.;
RT   "Inhibition of bacterial undecaprenyl pyrophosphate synthase by small
RT   fungal molecules.";
RL   J. Antibiot. 69:798-805(2016).
CC   -!- FUNCTION: Prenyltransferase; part of the gene cluster that mediates the
CC       biosynthesis of viridicatumtoxin, a tetracycline-like fungal
CC       meroterpenoid with a unique, fused spirobicyclic ring system
CC       (PubMed:20534346). The first step of the pathway is the production of
CC       the malonamoyl-CoA starter unit for the polyketide synthase vrtA
CC       (PubMed:20534346). The aldolase vrtJ may be involved in the synthesis
CC       of the malonamate substrate for malonamoyl-CoA synthetase vrtB
CC       (PubMed:20534346). The polyketide synthase vrtA then may utilize the
CC       malonamoyl-CoA starter unit, followed by sequential condensation of
CC       eight malonyl-CoA units to form the polyketide backbone
CC       (PubMed:20534346). The cyclization of the last ring could be mediated
CC       by the lactamase-like protein vrtG (PubMed:20534346). The proposed
CC       post-PKS tailoring steps are an hydroxylation at C5 catalyzed the
CC       cytochrome P450 monooxygenase vrtE, a hydroxylation at C12a catalyzed
CC       by VrtH and/or VrtI, and an O-methylation by the O-methyltransferase
CC       vrtF (PubMed:20534346, PubMed:24161266). VrtC is then proposed to
CC       catalyze the transfer of a geranyl group synthesized by vrtD to the
CC       aromatic C ring of the tetracyclic polyketide intermediate of
CC       viridicatumtoxin to yield previridicatumtoxin (PubMed:20534346).
CC       Finally, the cytochrome P450 monooxygenase vrtK catalyzes the
CC       spirocyclization of the geranyl moiety of previridicatumtoxin to afford
CC       viridicatumtoxin (PubMed:24161266). {ECO:0000269|PubMed:20534346,
CC       ECO:0000269|PubMed:24161266}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:20534346}.
CC   -!- BIOTECHNOLOGY: Viridicatumtoxin and its derivative, viridicatumtoxin B,
CC       exhibit anti-methicillin-resistant Staphylococcus aureus (anti-MRSA)
CC       activity (PubMed:19168978). Moreover, viridicatumtoxin and a C2 acetyl
CC       analog, spirohexaline, have been demonstrated to inhibit bacterial
CC       undecaprenyl diphosphate synthase, a potential new target for
CC       antibiotic development (PubMed:27049441). {ECO:0000269|PubMed:19168978,
CC       ECO:0000269|PubMed:27049441}.
CC   -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; GU574477; ADI24928.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7PHZ4; -.
DR   SMR; D7PHZ4; -.
DR   BioCyc; MetaCyc:MON-19282; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd13929; PT-DMATS_CymD; 1.
DR   InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR   PANTHER; PTHR40627; PTHR40627; 1.
DR   Pfam; PF11991; Trp_DMAT; 1.
DR   TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE   1: Evidence at protein level;
KW   Transferase.
FT   CHAIN           1..483
FT                   /note="Prenyltransferase vrtC"
FT                   /id="PRO_0000436830"
SQ   SEQUENCE   483 AA;  53237 MW;  1C852DAFFDA35360 CRC64;
     MGDATATEVF PVMDSIAVAM GDVESQLRVF HNVSRFLPTD DANQVFWWRT TGRHFAIMMH
     EARYSEARQV ELLLFYRFVI APRLGPRPTS ATPWFHSRVA PGIGDGSPIG YSWRWGTGPD
     TKPLIRHYIE AIGPLTGTTA DPLNEFAAKE MLYQLGQLVP GVELPLAWKF AAHIRPSLTD
     EPTRAVAGSS ILIGLQCAPE SAGIEVMAGL MTRSPAQVPE LLHSIFPRAM RDAYGPDASL
     DGLNMVRDFV CHDPQGQYLT ILGTTAIDCC AAASSRFKVY VTTTNTSFAH LAAVMTLGGR
     KPEAPESLTQ LQELWYALKG LDPEFPVTAE PLSSVCGAAN GTASGNPNAN VSGVTFYFDI
     HPKYPFPHIK LQVDISKHTI SDLGAINAVT EFLARRGQAA DAQAYLNVVR AMVPDEELRT
     RRGLQAFFAF AFKNGAVDIT SYFLPQIYRR YAEVQAELEP RKDCQGRSEL SSKLQRRSRF
     DSY