ID   DPCHF_COLHI             Reviewed;         473 AA.
AC   H1VQW0;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=FAD-dependent oxidoreductase dpchF {ECO:0000303|PubMed:32286350};
DE            EC=1.21.-.- {ECO:0000269|PubMed:32286350};
DE   AltName: Full=Diterpenoid pyrone biosynthesis cluster protein F {ECO:0000303|PubMed:32286350};
DE   Flags: Precursor;
GN   Name=dpchF {ECO:0000303|PubMed:32286350};
GN   ORFNames=CH063_12564, CH63R_05482;
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063;
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063;
RA   O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT   "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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: FAD-dependent oxidoreductase; part of the gene cluster that
CC       mediates the biosynthesis of the diterpenoid pyrones higginsianins A
CC       and B (PubMed:32286350). The first step of the pathway is the synthesis
CC       of the alpha-pyrone moiety by the polyketide synthase dpchA 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 dpchD
CC       through the action of the prenyltransferase dpchC 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 dpchE, and is followed by a
CC       cyclization cascade catalyzed by the terpene cyclase dpchB (Probable).
CC       The short chain dehydrogenase/reductase dpchG then oxidizes the 8S
CC       hydroxy group to a ketone and the short chain dehydrogenase/reductase
CC       dpchH reduces the ketone to the 8R hydroxy group to yield higginsianin
CC       B (PubMed:32286350). Finally, the FAD-dependent oxidoreductase dpchF
CC       converts higginsianin B into higginsianin A (PubMed:32286350).
CC       {ECO:0000269|PubMed:32286350, ECO:0000305|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 higginsianin A shows anti-HIV activity.
CC       {ECO:0000269|PubMed:32286350}.
CC   -!- SIMILARITY: Belongs to the beta-cyclopiazonate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CACQ02005519; CCF42616.1; -; Genomic_DNA.
DR   EMBL; LTAN01000004; OBR09790.1; -; Genomic_DNA.
DR   RefSeq; XP_018158307.1; XM_018300457.1.
DR   AlphaFoldDB; H1VQW0; -.
DR   SMR; H1VQW0; -.
DR   EnsemblFungi; CCF42616; CCF42616; CH063_12564.
DR   GeneID; 28864564; -.
DR   eggNOG; ENOG502R1TU; Eukaryota.
DR   HOGENOM; CLU_028280_0_0_1; -.
DR   OrthoDB; 569857at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   Proteomes; UP000092177; Chromosome 4.
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; Reference proteome;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..473
FT                   /note="FAD-dependent oxidoreductase dpchF"
FT                   /id="PRO_5010497735"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   473 AA;  50041 MW;  F55B664135600AC4 CRC64;
     MKLSFIASPV WALALAQFAA ATQVKIDVDV AIFGGGSAGI HAAIQLRDAG ATVAVIEKKS
     QIGGHAETYT DPQGKSTNVG VVVFDNIEVA SNYFARLNVS IVRGSPLGTA GPTYTYDFTS
     GAQIPAVNTS AEAQQQLTAA LQSYSTNVLS KYPWIDEGFL VPDPVPEELT IPFGELAQKY
     NFTALMPTIA MYNYFTGDLS TIPSLYGIKG LGQGALKNLF GSFILPASGK TRDLYDAAAI
     ELGNSVLLNA DVVKVQRDVR INSTTTGVTV LIQQPGQPPK LIRARKLLVA APPTLENVGA
     FDLTAEERGL ISKFSSLGCW ASVANVPGLN VTLKNYGVHM PYNQPSIPGP YGFVAYGSPN
     NFLVTVGLPD AANTAAKGEA VVRQSLATLS AVGAVPADAL EKLTFPFSAV HSPYSLRVSA
     EEIKAGFYSK FLALEGARNT YWTGAVWAGH NSALIWNFNM GTVLPGLKKD LGL