ID   DPASB_ARTSH             Reviewed;         243 AA.
AC   P9WEX1;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   25-MAY-2022, entry version 3.
DE   RecName: Full=Terpene cyclase dpasB {ECO:0000303|PubMed:32286350};
DE            EC=4.2.3.- {ECO:0000269|PubMed:32286350};
DE   AltName: Full=Diterpenoid pyrone biosynthesis cluster protein B {ECO:0000303|PubMed:32286350};
GN   Name=dpasB {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: Terpene cyclase; part of the gene cluster that mediates the
CC       biosynthesis of the diterpenoid pyrones subglutinols A and B
CC       (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   -!- 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 paxB family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P9WEX1; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR039020; PaxB-like.
DR   PANTHER; PTHR42038; PTHR42038; 1.
PE   1: Evidence at protein level;
KW   Lyase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..243
FT                   /note="Terpene cyclase dpasB"
FT                   /id="PRO_0000451527"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   243 AA;  28019 MW;  3598ECB9DF543C7D CRC64;
     MDVHDLTRAP PEYLEVVWVT DVCKLVMAVG WLSNYIGMIA KSIKEQTYSM ALMPLCCNFA
     WEFTYFFIYP YKVPMERNIH TLAFLLNCGV MYTAVRYGAR EWGHAPLVQR NLPVIFVVCI
     ACWVSAHVAF AEQYGPSLAQ AVSGFACQIL LSAGGTCQLL CRGHSRGASY KLWLARFMGS
     FALILPNMLR YKYWRDDHQY IGSPLYIWFL GMFLFLDGSY GFVLWYVRRH EREQVLVAKP
     KVQ