DPMAE_METAN
ID DPMAE_METAN Reviewed; 472 AA.
AC P9WEY1;
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 dpmaE {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=dpmaE {ECO:0000303|PubMed:32286350};
OS Metarhizium anisopliae (Entomophthora anisopliae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=5530;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25263348; DOI=10.1186/1471-2164-15-822;
RA Staats C.C., Junges A., Guedes R.L., Thompson C.E., de Morais G.L.,
RA Boldo J.T., de Almeida L.G., Andreis F.C., Gerber A.L., Sbaraini N.,
RA da Paixao R.L., Broetto L., Landell M., Santi L., Beys-da-Silva W.O.,
RA Silveira C.P., Serrano T.R., de Oliveira E.S., Kmetzsch L., Vainstein M.H.,
RA de Vasconcelos A.T., Schrank A.;
RT "Comparative genome analysis of entomopathogenic fungi reveals a complex
RT set of secreted proteins.";
RL BMC Genomics 15:822-822(2014).
RN [2]
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 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 dpmaA 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 dpmaD
CC through the action of the prenyltransferase dpmaC 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 dpmaE, and is followed by a
CC cyclization cascade catalyzed by the terpene cyclase dpmaB (Probable).
CC The dehydrogenase dpmaF is then involved in tetrahydrofuran (THF) ring
CC formation at the C5 unit to complete the formation of subglutinols A
CC and B (PubMed:32286350). {ECO:0000269|PubMed:32286350,
CC 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: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 EMBL; JNNZ01000128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P9WEY1; -.
DR SMR; P9WEY1; -.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..472
FT /note="FAD-dependent monooxygenase dpmaE"
FT /id="PRO_0000451545"
FT TRANSMEM 440..460
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 230..232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 305
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 315..319
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"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 472 AA; 53383 MW; 03DB85E8EE1D13CC CRC64;
MSQRQFKVII IGGSVTGLTL AHSLHKIGID YVVLEKRDTV TPQEGASIGI LPNGARILDQ
LGLYEAIEDE APPLGATRIH FPDGFAFTSL YPKRMRHSFG YPIAFLERRQ LLRILYDALP
DKTRIHVNKT MSTIEHFTKD EITGARVLTK EGDVYEGDLI VGADGIHSQT RGEIWRRINS
SKSAFKTAEE YSCCFGISKC VTGLIAGEQV MHMRNGRTLV VIPSKDEVVF WFLVEKLDRK
YTYSEAPRFT IDDATALCSQ VFTLPIGNNI KFEDVWNKRE VVNMLSLEES CLSTWSTGRL
VCIGDSIHKM TVNLGQGANC AIEDVAVLCN LLRNMCQLKS GTRPTEQEID LLLRRFNKQH
LSRVTQITNM SKLTVRVHAR KGVLHRLVGR YVMPYFGAYF EARPFNMLAD AASLDFIPLP
KSSYPGWEKY SSKTRGNSRL LPLMFTLPLL YFGLSWIVGI YWKPGYLHAW NS
