DPMPB_MACPH
ID DPMPB_MACPH Reviewed; 243 AA.
AC K2RU64;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Terpene cyclase dpmpB {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=dpmpB {ECO:0000303|PubMed:32286350}; ORFNames=MPH_09195;
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6;
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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 diterpenoid pyrones (PubMed:32286350). The first step
CC of the pathway is the synthesis of the alpha-pyrone moiety by the
CC polyketide synthase dpmpA via condensation of one acetyl-CoA starter
CC unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-
CC pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed
CC by the GGPP synthase dpmpD through the action of the prenyltransferase
CC dpmpC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent
CC steps in the diterpenoid pyrone biosynthetic pathway involve the
CC decalin core formation, which is initiated by the epoxidation of the
CC C10-C11 olefin by the FAD-dependent oxidoreductase dpmpE, and is
CC followed by a cyclization cascade catalyzed by the terpene cyclase
CC dpmpB (Probable). The short chain dehydrogenase/reductase dpmpG then
CC oxidizes the 8S hydroxy group to a ketone and the short chain
CC dehydrogenase/reductase dpmpH reduces the ketone to the 8R hydroxy
CC group to yield higginsianin B (PubMed:32286350). Higginsianin B is
CC further methylated by the methyltransferase dpmpI to produce the
CC intermediate named FDDP B (PubMed:32286350). The cytochrome P450
CC monooxygenase dpmpJ then oxidizes the C-26 methyl to primary alcohol,
CC producing the final diterpenoid pyrone with a C-26 primary alcohol on
CC the gamma-pyrone moiety named FDDP C (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 FDDP C shows anti-cancer and anti-HIV activities
CC (PubMed:32286350). FDDP C shows also inhibitory activity of 42-mer-
CC amyloid beta aggregation that is involved in the pathogenesis of
CC Alzheimer's disease (PubMed:32286350). {ECO:0000269|PubMed:32286350}.
CC -!- SIMILARITY: Belongs to the paxB family. {ECO:0000305}.
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DR EMBL; AHHD01000387; EKG13729.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RU64; -.
DR EnsemblFungi; EKG13729; EKG13729; MPH_09195.
DR eggNOG; ENOG502RZAD; Eukaryota.
DR HOGENOM; CLU_087059_0_1_1; -.
DR InParanoid; K2RU64; -.
DR OrthoDB; 1094347at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
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; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..243
FT /note="Terpene cyclase dpmpB"
FT /id="PRO_0000451531"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
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; 27934 MW; 12E871B2D5B9244B CRC64;
MNIVPLSQAP PEFLEVAWLA DACKLLMGVG WTANYIGMIY KSIKDRTYGM ALMPLCCNFA
WELVYALILP FDSGMEKWVH VTGLAFNCGV MYTAIKFAPG EWAHARLVQR HLTWIFIASV
AGWMSAHLAL AAQLGPSLAQ AWSAYGCQLL LSVGGLCQLL CRGHSRGTSY LLWFSRFFGS
LVLIPQDILR YKYWRRDHEW MKSPLYLWFV SIFLILDGSY GILLWYVRRF ERETAEAENR
KRR
