DPASE_ARTSH
ID DPASE_ARTSH Reviewed; 476 AA.
AC P9WEX4;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=FAD-dependent monooxygenase dpasE {ECO:0000303|PubMed:32286350};
DE EC=1.-.-.- {ECO:0000269|PubMed:32286350};
DE AltName: Full=Diterpenoid pyrone biosynthesis cluster protein E {ECO:0000303|PubMed:32286350};
DE Flags: Precursor;
GN Name=dpasE {ECO:0000303|PubMed:32286350};
OS Arthrinium sacchari (Coniosporium sacchari).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Apiosporaceae; Apiospora.
OX NCBI_TaxID=166626;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP 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: FAD-dependent monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the diterpenoid pyrones subglutinols A and
CC B (PubMed:32286350). The first step of the pathway is the synthesis of
CC the alpha-pyrone moiety by the polyketide synthase dpasA via
CC condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units
CC and 2 methylations (PubMed:32286350). The alpha-pyrone is then combined
CC with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase
CC dpasD through the action of the prenyltransferase dpasC to yield a
CC linear alpha-pyrone diterpenoid (PubMed:32286350). Subsequent steps in
CC the 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 dpasE, and is followed by a
CC cyclization cascade catalyzed by the terpene cyclase dpasB
CC (PubMed:32286350). The FAD-linked oxidoreductase dpasF is then involved
CC in tetrahydrofuran (THF) ring formation at the C5 unit to complete the
CC formation of subglutinols A and B (PubMed:32286350). DpasF possesses
CC also an additional catalytic ability of multi-step oxidations to
CC generate a new DDP analog with an enone system at the C5 named FDDP A
CC (PubMed:32286350). {ECO:0000269|PubMed:32286350}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:32286350}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-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 paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P9WEX4; -.
DR SMR; P9WEX4; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..476
FT /note="FAD-dependent monooxygenase dpasE"
FT /id="PRO_0000451542"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 233..235
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 318..322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 476 AA; 53436 MW; D9E8FD2BFD3E450D CRC64;
MSQPAFKIII VGCSVTGLTL AHCLDKLGVE YTILEKRSAV VLQEGASVAV MPNGGRILDQ
LGLYDAFEKA TVPLDLTDAY LPDQDFRFTS DYPRRVLATF GYPVAFMERR GLLEILYDGI
ADKSKIHLNK GVTHVEQNDD GAKVHTEDGE VYEGDIVVGA DGIHSKTLRE MWRMMGEPVV
NGIAQSESQN MSVAFSCVFG ISHDVPELQP GEQILRMCNG STIFVMGSKG VVFWFIVTQL
NRRYEYHDAP RYTTEEAAAF CEARKDAEIK EGVTFECIWR KQHVFNMLPL QESLFQTWSH
GRVVCIGDSV HKMTINLGQG ANCAIEDVTV LCNMLRAFLA EKREKKPSYS EIDTLLRRFN
KEHLPRASTI VETSRLTTRV HAQVGISQRI MTRWVVPYFG KFLQGKPLGL IASGPVLDFL
PLKRASYPGW ERYRVKKSSR GAGFWITAFL SLSLLAVAAT MYGWGNSQIW ADWNIL