DPMAC_METAN
ID DPMAC_METAN Reviewed; 295 AA.
AC P9WEX8;
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=Polyprenyl transferase dpmaC {ECO:0000303|PubMed:32286350};
DE EC=2.5.1.- {ECO:0000305|PubMed:32286350};
DE AltName: Full=Diterpenoid pyrone biosynthesis cluster protein C {ECO:0000303|PubMed:32286350};
GN Name=dpasC {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: Polyprenyl transferase; 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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P32378};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:32286350}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-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 UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; JNNZ01000128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P9WEX8; -.
DR SMR; P9WEX8; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 1: Evidence at protein level;
KW Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..295
FT /note="Polyprenyl transferase dpmaC"
FT /id="PRO_0000451535"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 295 AA; 32948 MW; 12D9C21B2A228FCE CRC64;
MPTRANKVET AWSALLAGAS ETRQEHLAPS PLFILRQTLF CVLAAYLFCG AGMVWNDWID
RDIDANVART KNRPLASGKV TTAQAFVWMA LQVIASCAVL HVMLDGKDVH VIPVMIASML
YPFLKRPTAK KLHIYPQYML AFTIAWPAIP GRAAICGRDE SFGETVRYCL PLCTVVFFWT
IYLNTAYSYQ DVVDDRKLNV NSFYNIAGRH THLVLVALVC PILACLPLYL TQFQSTWLWV
TWMGVWTAAF AVQLALFDAK QPASGGSLHK SNFVLGIWTI VVCSVELLLK ARVSI
