DPMPI_MACPH
ID DPMPI_MACPH Reviewed; 196 AA.
AC K2RGJ8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=O-methyltransferase dpmpI {ECO:0000303|PubMed:32286350};
DE EC=2.1.1.- {ECO:0000269|PubMed:32286350};
DE AltName: Full=Diterpenoid pyrone biosynthesis cluster protein I {ECO:0000303|PubMed:32286350};
GN Name=dpmpI {ECO:0000303|PubMed:32286350}; ORFNames=MPH_09194;
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, CATALYTIC ACTIVITY, 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: O-methyltransferase; part of the gene cluster that mediates
CC the biosynthesis of diterpenoid pyrones (PubMed:32286350). The first
CC step 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:0000269|PubMed:32286350}.
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 class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {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 EMBL; AHHD01000387; EKG13728.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RGJ8; -.
DR SMR; K2RGJ8; -.
DR EnsemblFungi; EKG13728; EKG13728; MPH_09194.
DR eggNOG; KOG3178; Eukaryota.
DR HOGENOM; CLU_129453_0_0_1; -.
DR InParanoid; K2RGJ8; -.
DR OrthoDB; 817726at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; Transferase.
FT CHAIN 1..196
FT /note="O-methyltransferase dpmpI"
FT /id="PRO_0000451555"
FT REGION 166..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127..128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
FT BINDING 152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 174..175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O04385"
SQ SEQUENCE 196 AA; 22191 MW; C8C848BF66CC1FF8 CRC64;
MVAETGTGLF SAHKITEELA STSLDSGVHL LFDIHDRTFQ ALPDFLAEHR YQEVNDIRNT
VFQKAFDTNL SIYEYLVHHP QLQAHMQDAM KLHQPEGDWL SVFPADEIVG NQQTAPDPAR
VLFVDIGGGM GQQCIRFRER YPDLAGRVIL QDIPQTINRV PKPMPNGIEA VPHSFEDPQP
IKSKSPRLDN LARERL
