MACG_PENTR
ID MACG_PENTR Reviewed; 319 AA.
AC A0A2P1DP87;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2018, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Polyprenyl transferase macG {ECO:0000303|PubMed:28926261};
DE EC=2.5.1.- {ECO:0000250|UniProtKB:G3Y418};
DE AltName: Full=Macrophorins biosynthesis cluster protein G {ECO:0000303|PubMed:28926261};
GN Name=macG {ECO:0000303|PubMed:28926261};
OS Penicillium terrestre.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=374132;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=LM2;
RX PubMed=28926261; DOI=10.1021/acs.orglett.7b02653;
RA Tang M.C., Cui X., He X., Ding Z., Zhu T., Tang Y., Li D.;
RT "Late-stage terpene cyclization by an integral membrane cyclase in the
RT biosynthesis of isoprenoid epoxycyclohexenone natural products.";
RL Org. Lett. 19:5376-5379(2017).
CC -!- FUNCTION: Polyprenyl transferase; part of the gene cluster that
CC mediates the biosynthesis of macrophorins, isoprenoid
CC epoxycyclohexenones containing cyclized drimane moieties
CC (PubMed:28926261). The first step of the pathway is the synthesis of 6-
CC methylsalicylic acid (6-MSA) by the polyketide synthase macA
CC (PubMed:28926261). 6-MSA is then converted to m-cresol by the
CC decarboxylase macB (By similarity). The cytochrome P450 monooxygenase
CC macC then catalyzes the oxidation of m-cresol to toluquinol (By
CC similarity). Epoxidation of toluquinol is then performed by the short
CC chain dehydrogenase macD, with the help of macE, and a further
CC prenylation by macG leads to 7-deacetoxyyanuthone A (By similarity).
CC The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by
CC the cytochrome P450 monooxygenase macH to yield 22-deacetylyanuthone A
CC (By similarity). O-Mevalon transferase macI then attaches mevalon to
CC the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E (By
CC similarity). The terpene cyclase macJ catalyzes the cyclization of 22-
CC deacetylyanuthone A to macrophorin A (PubMed:28926261). MacJ is also
CC able to catalyze cyclization of yanuthone E and 7-deacetoxyyanuthone A
CC to their corresponding macrophorins (PubMed:28926261). The macJ
CC products can be further modified by macH and macJ, as well as by the
CC FAD-dependent monooxygenase macF, to produce additional macrophorins,
CC including 4'-oxomacrophorin A, 4'-oxomacrophorin D and 4'-
CC oxomacrophorin E (PubMed:28926261). {ECO:0000250|UniProtKB:G3Y418,
CC ECO:0000269|PubMed:28926261}.
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:28926261}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- MISCELLANEOUS: The macrophorins cluster contains a single gene
CC insertion (encoding for the terpene cyclase macJ) compared with the
CC yanuthone cluster that produces the linear compound yanuthone.
CC {ECO:0000269|PubMed:28926261}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; MF989998; AVK70099.1; -; Genomic_DNA.
DR EMBL; MH388470; QBC75449.1; -; Genomic_DNA.
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; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
PE 3: Inferred from homology;
KW Magnesium; Membrane; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..319
FT /note="Polyprenyl transferase macG"
FT /id="PRO_0000454091"
FT TRANSMEM 28..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 319 AA; 35412 MW; 34C64620FC1E346D CRC64;
MTVSTTPKSQ RNVARGVWEL ARLHTREAWL CWYPAIWGAC VAAGMRDVSL ELAPFLRLLF
GIWASVTATH CAFCTFNDIC DQKLDKHVER CKIRPLPSGM ISTSEAVVAF ICWLPVTLAI
TWGTLGPAVM AGFIPVWVLS TIYPFMKRIM PFPQVVLGAI IGGAVFPGWV GITGDLKDLD
QALPLFFATA SWVVYFDVFY ATQDRPDDEK IGVKSLAVLL GKNVQILLAV LGALQVLLFA
VTALRADMSL IFWVLGLGVW MVNVPWHILS LDLKDRHSGG RIFKSNIKLG LYLTGVSLLE
LFVVRVYDIS LANMKMELH
