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DPMPG_MACPH
ID   DPMPG_MACPH             Reviewed;         175 AA.
AC   K2RLM6;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Short chain dehydrogenase/reductase dpmpG {ECO:0000303|PubMed:32286350};
DE            EC=1.1.1.- {ECO:0000269|PubMed:32286350};
DE   AltName: Full=Diterpenoid pyrone biosynthesis cluster protein G {ECO:0000303|PubMed:32286350};
GN   Name=dpmpG {ECO:0000303|PubMed:32286350}; ORFNames=MPH_09198;
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: Short chain dehydrogenase/reductase; part of the gene cluster
CC       that mediates the biosynthesis of diterpenoid pyrones
CC       (PubMed:32286350). The first step of the pathway is the synthesis of
CC       the alpha-pyrone moiety by the polyketide synthase dpmpA 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 dpmpD
CC       through the action of the prenyltransferase dpmpC 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 dpmpE, and is followed by a
CC       cyclization cascade catalyzed by the terpene cyclase dpmpB (Probable).
CC       The short chain dehydrogenase/reductase dpmpG then oxidizes the 8S
CC       hydroxy group to a ketone and the short chain dehydrogenase/reductase
CC       dpmpH reduces the ketone to the 8R hydroxy group to yield higginsianin
CC       B (PubMed:32286350). Higginsianin B is further methylated by the
CC       methyltransferase dpmpI to produce the intermediate named FDDP B
CC       (PubMed:32286350). The cytochrome P450 monooxygenase dpmpJ then
CC       oxidizes the C-26 methyl to primary alcohol, producing the final
CC       diterpenoid pyrone with a C-26 primary alcohol on the gamma-pyrone
CC       moiety named FDDP C (PubMed:32286350). {ECO:0000269|PubMed:32286350,
CC       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 short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AHHD01000387; EKG13732.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2RLM6; -.
DR   SMR; K2RLM6; -.
DR   STRING; 1126212.K2RLM6; -.
DR   EnsemblFungi; EKG13732; EKG13732; MPH_09198.
DR   eggNOG; KOG0725; Eukaryota.
DR   HOGENOM; CLU_010194_2_19_1; -.
DR   InParanoid; K2RLM6; -.
DR   OrthoDB; 1910691at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000007129; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..175
FT                   /note="Short chain dehydrogenase/reductase dpmpG"
FT                   /id="PRO_0000451550"
FT   BINDING         44
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT   BINDING         71..72
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
FT   BINDING         98
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZNN8"
SQ   SEQUENCE   175 AA;  18066 MW;  D2F087CFD2225FED CRC64;
     MSASSTEATN LAGKTCLITG GAGGLGRALA AAFLRAGANV AICDLNEERL KQASAELSGT
     GAGSLLAANA DVADPAAAQQ LFDRITAKFR TVDVLVNNAA IMDRFDPVAD LDHELWDRVI
     SVNLAGPFIF SKLALRVMLQ QPKPDGCILN IASGAAKGGW LAGRCDLGLA RICRG
 
 
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