DPMAF_METAN
ID DPMAF_METAN Reviewed; 509 AA.
AC P9WEY2;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 25-MAY-2022, entry version 6.
DE RecName: Full=FAD-linked oxidoreductase dpmaF {ECO:0000303|PubMed:32286350};
DE EC=1.1.1.- {ECO:0000269|PubMed:32286350};
DE AltName: Full=Diterpenoid pyrone biosynthesis cluster protein F {ECO:0000303|PubMed:32286350};
DE Flags: Precursor;
GN Name=dpmaF {ECO:0000303|PubMed:32286350}; ORFNames=MANI_006343;
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, 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-linked 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 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 -!- 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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; JNNZ01000128; KFG81918.1; -; Genomic_DNA.
DR AlphaFoldDB; P9WEY2; -.
DR SMR; P9WEY2; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..509
FT /note="FAD-linked oxidoreductase dpmaF"
FT /id="PRO_0000451547"
FT DOMAIN 59..231
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 509 AA; 55404 MW; 444BC430E5B83EB3 CRC64;
MTRLSLQLIA GLAGQAWLVN SDTPSHEAFA SCLSDASVPI ATKGTPEWTQ HTTPFNTRLQ
YEPIAVAVPT EISQIAAAVT CAKKNSIPVT AKSGGHSFTS LGLGGEDGHL VIQLDRMYNV
ELAQNGTARI QSGARLGHVA VELYNQGKRA LSHGYCPAVG VGGHAAHGGY GMVSRKYGLT
LDWMKDATVV LHNGTIVYCS ESEHSDLFWA IRGAGSSFGI VAEYGFETFP APEKVTNFGI
VLDWNPETAP AGLLAFQDFA QTMPSELSCQ IDVRSTGYTL NGSYVGNEAS LREALVPLLG
KIGGHLEVHE GNWLEYVKFW AFGQPNIDIT PPADNVHLSL YTTGALTPSL SANQFKSFAD
YIAKDAIKRG NSWSIQMFIH GGQNSAISGP KITDTAYAHR DKFLIFQFTD FVWPSQEYPE
DGLALGREFR DIITNSFTND QWGMYANVPD SQLSSGEAQK LYWGKNLERL ETIKAKYDPS
NLFRNPQSVK AAARCATHPL LLQGQCLLF
