ID   DPCHB_COLHI             Reviewed;         242 AA.
AC   A0A1B7YCX1;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Terpene cyclase dpchB {ECO:0000303|PubMed:32286350};
DE            EC=4.2.3.- {ECO:0000305|PubMed:32286350};
DE   AltName: Full=Diterpenoid pyrone biosynthesis cluster protein B {ECO:0000303|PubMed:32286350};
GN   Name=dpchB {ECO:0000303|PubMed:32286350}; ORFNames=CH63R_05476;
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063;
RA   O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT   "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, PATHWAY, 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 higginsianins 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 dpchA via
CC       condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units
CC       and 2 methylations (Probable). The alpha-pyrone is then combined with
CC       geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD
CC       through the action of the prenyltransferase dpchC to yield a linear
CC       alpha-pyrone diterpenoid (Probable). Subsequent steps in the
CC       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 dpchE, and is followed by a
CC       cyclization cascade catalyzed by the terpene cyclase dpchB (Probable).
CC       The short chain dehydrogenase/reductase dpchG then oxidizes the 8S
CC       hydroxy group to a ketone and the short chain dehydrogenase/reductase
CC       dpchH reduces the ketone to the 8R hydroxy group to yield higginsianin
CC       B (PubMed:32286350). Finally, the FAD-dependent oxidoreductase dpchF
CC       converts higginsianin B into higginsianin A (PubMed:32286350).
CC       {ECO:0000269|PubMed:32286350, ECO:0000305|PubMed:32286350}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|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 higginsianin A shows anti-HIV activity.
CC       {ECO:0000269|PubMed:32286350}.
CC   -!- SIMILARITY: Belongs to the paxB family. {ECO:0000305}.
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DR   EMBL; LTAN01000004; OBR09784.1; -; Genomic_DNA.
DR   RefSeq; XP_018158301.1; XM_018300451.1.
DR   AlphaFoldDB; A0A1B7YCX1; -.
DR   GeneID; 28864558; -.
DR   OrthoDB; 1094347at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000092177; Chromosome 4.
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..242
FT                   /note="Terpene cyclase dpchB"
FT                   /id="PRO_0000451528"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   242 AA;  27487 MW;  597341B072912F33 CRC64;
     MNVADISQAP EAYRDVVWIA DTCKLIMGIG WTANYVGMIR KSLKDQTYAM ALLPLCCNFA
     WELTYAIMYA FTTSLEKYVH FSGLLLNCGV MYTAVKNAPR EWEHAPLVQR NLRLIFVLAV
     AGFASAHVVL AKQVGPELGQ AWSAYACQLL LSVGGLCQLL CRGHSRGASY FLWFSRFFGS
     LVLVPQDIIR YTYWKEAHEF MGSPMYIWFV TIFLILDGSY GLCLWYVRRF EQQNPAAGKL
     KK