ID   DPMAB_METAN             Reviewed;         243 AA.
AC   P9WEX7;
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 dpmaB {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=dpmaB {ECO:0000303|PubMed:32286350}; ORFNames=MANI_006367;
OS   Metarhizium anisopliae (Entomophthora anisopliae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=5530;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=25263348; DOI=10.1186/1471-2164-15-822;
RA   Staats C.C., Junges A., Guedes R.L., Thompson C.E., de Morais G.L.,
RA   Boldo J.T., de Almeida L.G., Andreis F.C., Gerber A.L., Sbaraini N.,
RA   da Paixao R.L., Broetto L., Landell M., Santi L., Beys-da-Silva W.O.,
RA   Silveira C.P., Serrano T.R., de Oliveira E.S., Kmetzsch L., Vainstein M.H.,
RA   de Vasconcelos A.T., Schrank A.;
RT   "Comparative genome analysis of entomopathogenic fungi reveals a complex
RT   set of secreted proteins.";
RL   BMC Genomics 15:822-822(2014).
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 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 dpmaA 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 dpmaD
CC       through the action of the prenyltransferase dpmaC 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 dpmaE, and is followed by a
CC       cyclization cascade catalyzed by the terpene cyclase dpmaB (Probable).
CC       The dehydrogenase dpmaF is then involved in tetrahydrofuran (THF) ring
CC       formation at the C5 unit to complete the formation of subglutinols A
CC       and B (PubMed:32286350). {ECO:0000269|PubMed:32286350,
CC       ECO:0000305|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}.
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DR   EMBL; JNNZ01000128; KFG81920.1; -; Genomic_DNA.
DR   AlphaFoldDB; P9WEX7; -.
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 dpmaB"
FT                   /id="PRO_0000451530"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
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        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   243 AA;  27857 MW;  4D33DA3D952DC5BD CRC64;
     MNAADISRAP PGYLEVAWIA DTCKLLMGLG WTTNYAGMIY KSLKDRTYGM ALMPLCCNFA
     WELTYAVIYP FGSRQDKFTH YFGLMLNCGV MYTAVKNAER EWTHAPLVRR NLPFIFIICI
     AAWTTAHLAL ALQIGPSHAQ AFSAYGCQLL LSVGALCQLL SRGSSRGASY FLWFCRFFGS
     LVLIPQDVLR YRYWRQDHEY MGSPLYIWFV SIFLLLDGSY ALCLWYVRRF ESEQEEAKKA
     KSI