ID   DPASF_ARTSH             Reviewed;         473 AA.
AC   P9WEX5;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=FAD-dependent oxidoreductase dpasF {ECO:0000303|PubMed:32286350};
DE            EC=1.1.1.- {ECO:0000269|PubMed:32286350};
DE   AltName: Full=Diterpenoid pyrone biosynthesis cluster protein E {ECO:0000303|PubMed:32286350};
DE   Flags: Precursor;
GN   Name=dpasF {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 oxidoreductase; 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;
CC         Evidence={ECO:0000250|UniProtKB:B8NI10};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:32286350}.
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 beta-cyclopiazonate dehydrogenase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P9WEX5; -.
DR   SMR; P9WEX5; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..473
FT                   /note="FAD-dependent oxidoreductase dpasF"
FT                   /id="PRO_0000451747"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        401
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   473 AA;  50300 MW;  6939B2823D2E19F1 CRC64;
     MNRLLASALL VGSAVVAPVS AACIKNATVT EVDVAIIGGG ASGVYAAARL IDNNKTVVVL
     ERNADRIGGQ TETYYDPTTG TPVNVGVKVF SNTTVTTDFL KRFDFPMGTL NVGQTLATGT
     QYVDFATGKL IPNFTAVVPA VQAAAMQRYA AELAKYPQIK FGYNLGPQVP EDLVLPFGKF
     MEKHNLTGMA QTMFEFNSGY TPLLEIPALY ILKYLDTYEL QSLQSGSFIV AANGDSATLY
     RNAAKFLGER VVYGVSGMHI QRSSAAGGRV TISVGNSTTG THMIRAKKLI VAAPPTLDNL
     RSTGLDLDTT EAGLFGKLSA GVFYSLVVKD TGVAKANLRN RHPANPYGFP DQPFIYSVIP
     LPKTSGLAQV LLGSASPLTA SQVEARVAAD IGRLPASLRG NATSVPKVVT MAAHTWNVMA
     PVADIKAGFY DKLEGLQGLK DTWYIGAAWA TQSSTTIWEG LEQEFLPKLL AAL