DPCHE_COLHI
ID DPCHE_COLHI Reviewed; 470 AA.
AC H1VM35;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=FAD-dependent monooxygenase dpchE {ECO:0000303|PubMed:32286350};
DE EC=1.-.-.- {ECO:0000305|PubMed:32286350};
DE AltName: Full=Diterpenoid pyrone biosynthesis cluster protein E {ECO:0000303|PubMed:32286350};
DE Flags: Precursor;
GN Name=dpchE {ECO:0000303|PubMed:32286350};
GN ORFNames=CH063_11613, CH63R_05475;
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, 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 monooxygenase; 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; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|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 higginsianin A shows anti-HIV activity.
CC {ECO:0000269|PubMed:32286350}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; CACQ02004606; CCF41288.1; -; Genomic_DNA.
DR EMBL; LTAN01000004; OBR09783.1; -; Genomic_DNA.
DR RefSeq; XP_018158300.1; XM_018300450.1.
DR AlphaFoldDB; H1VM35; -.
DR SMR; H1VM35; -.
DR STRING; 80884.CCF41288; -.
DR EnsemblFungi; CCF41288; CCF41288; CH063_11613.
DR GeneID; 28864557; -.
DR eggNOG; KOG2614; Eukaryota.
DR HOGENOM; CLU_009665_12_2_1; -.
DR OrthoDB; 462247at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR Proteomes; UP000092177; Chromosome 4.
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 Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..470
FT /note="FAD-dependent monooxygenase dpchE"
FT /id="PRO_0000451543"
FT TRANSMEM 447..463
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 131
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 237..239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 312
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 322..326
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 470 AA; 52266 MW; 167250A6283FD688 CRC64;
MSEPHFKVII VGGSITGLTL AHSLHKIGVD FTILEKRATV TPQEGASVGI LPNGARVLDQ
LGLYGLVEEA TAPLGATHIH FPDGFHFCSL YPKSMLDNFG YPVAFLERRR LLEVLYNALP
DKSKVLVNKT VSDIEQCEDG KSAGVKVRTA DGDVYEGDIV VGADGVHSRT RSELWRMSSS
AGQSEDVRME KARMSAEYSC VFGISRGPSG LKAGEQIMRM YDGRTLVVIP SKDDVVFWFL
SRKLGKKYKY SEAPRFTLED AAAECAELAD APLGNDVRFG DVWKIRQTFN MVVLEENLLR
TWSFGRVLCI GDSIHKMTVN LGQGANCAIE DVAILTNLLS QCLGSKREAK PSGQELDALL
RRFNDVHLSR VSHIYDTSWL IARVHARDGF VRKIIGRYVM PYFGHKFESR PFNMIANAAA
LEFLPLPRSS FPGWEKYKSK EDKSGSWAVV SRSVLLLVGL AILSTWWRRA
