ID   DPASC_ARTSH             Reviewed;         336 AA.
AC   P9WEX2;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   03-AUG-2022, entry version 6.
DE   RecName: Full=Polyprenyl transferase dpasC {ECO:0000303|PubMed:32286350};
DE            EC=2.5.1.- {ECO:0000269|PubMed:32286350};
DE   AltName: Full=Diterpenoid pyrone biosynthesis cluster protein C {ECO:0000303|PubMed:32286350};
GN   Name=dpasC {ECO:0000303|PubMed:32286350};
OS   Arthrinium sacchari (Coniosporium sacchari).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Apiosporaceae; Apiospora.
OX   NCBI_TaxID=166626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   AND BIOTECHNOLOGY.
RX   PubMed=32286350; DOI=10.1038/s41467-020-15664-4;
RA   Tsukada K., Shinki S., Kaneko A., Murakami K., Irie K., Murai M.,
RA   Miyoshi H., Dan S., Kawaji K., Hayashi H., Kodama E.N., Hori A., Salim E.,
RA   Kuraishi T., Hirata N., Kanda Y., Asai T.;
RT   "Synthetic biology based construction of biological activity-related
RT   library of fungal decalin-containing diterpenoid pyrones.";
RL   Nat. Commun. 11:1830-1830(2020).
CC   -!- FUNCTION: Polyprenyl transferase; part of the gene cluster that
CC       mediates the biosynthesis of the diterpenoid pyrones subglutinols A and
CC       B (PubMed:32286350). The first step of the pathway is the synthesis of
CC       the alpha-pyrone moiety by the polyketide synthase dpasA via
CC       condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units
CC       and 2 methylations (PubMed:32286350). The alpha-pyrone is then combined
CC       with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase
CC       dpasD through the action of the prenyltransferase dpasC to yield a
CC       linear alpha-pyrone diterpenoid (PubMed:32286350). Subsequent steps in
CC       the diterpenoid pyrone biosynthetic pathway involve the decalin core
CC       formation, which is initiated by the epoxidation of the C10-C11 olefin
CC       by the FAD-dependent oxidoreductase dpasE, and is followed by a
CC       cyclization cascade catalyzed by the terpene cyclase dpasB
CC       (PubMed:32286350). The FAD-linked oxidoreductase dpasF is then involved
CC       in tetrahydrofuran (THF) ring formation at the C5 unit to complete the
CC       formation of subglutinols A and B (PubMed:32286350). DpasF possesses
CC       also an additional catalytic ability of multi-step oxidations to
CC       generate a new DDP analog with an enone system at the C5 named FDDP A
CC       (PubMed:32286350). {ECO:0000269|PubMed:32286350}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P32378};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:32286350}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- BIOTECHNOLOGY: Diterpenoid pyrones display various biological
CC       activities and subglutinol A shows insecticidal and anti-HIV
CC       activities. {ECO:0000269|PubMed:32286350}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P9WEX2; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd13959; PT_UbiA_COQ2; 1.
DR   Gene3D; 1.10.357.140; -; 1.
DR   InterPro; IPR039653; Prenyltransferase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR   InterPro; IPR044878; UbiA_sf.
DR   PANTHER; PTHR11048; PTHR11048; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   PROSITE; PS00943; UBIA; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..336
FT                   /note="Polyprenyl transferase dpasC"
FT                   /id="PRO_0000451532"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        66
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   336 AA;  37916 MW;  705169C83E4F5F96 CRC64;
     MASVAKARSP KSTQSNSLVY DLLVLSRFTK YNPLFTIFAG GMFLFVASFP TTAFSCLLAG
     STLVGNGSDV TLTWVFRQTA LCLSACYSFC GAGMVWNDWI DRDIDANVAR TKDRPLASGR
     VTTTQAMLWM VFQMAVSWWL LHFMLDGKDV NNHMLPVVIG SFLYPFGKRP ICSKFYFYPQ
     YILGFTIAWP AVPGRTAIFH GQETFAESVQ ACMPLLNMVF FWTIFLNTAY SYQDVVDDRK
     MGVNSFYNVL GKHVHLLLCL LLVPVAVCVP MYLNQFHSTW LWVSWAGVWA LSLLRQITRF
     DEKNPASGGS LHVDNFLLGA WTVVACTIEL LMRYYS