ID   MACI_PENTR              Reviewed;         431 AA.
AC   A0A2P1DP75;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=O-Mevalon transferase macI {ECO:0000303|PubMed:28926261};
DE            EC=2.-.-.- {ECO:0000250|UniProtKB:G3Y421};
DE   AltName: Full=Macrophorins biosynthesis cluster protein I {ECO:0000303|PubMed:28926261};
GN   Name=macI {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: O-Mevalon transferase; part of the gene cluster that mediates
CC       the biosynthesis of macrophorins, isoprenoid epoxycyclohexenones
CC       containing cyclized drimane moieties (PubMed:28926261). The first step
CC       of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by
CC       the polyketide synthase macA (PubMed:28926261). 6-MSA is then converted
CC       to m-cresol by the decarboxylase macB (By similarity). The cytochrome
CC       P450 monooxygenase macC then catalyzes the oxidation of m-cresol to
CC       toluquinol (By similarity). Epoxidation of toluquinol is then performed
CC       by the short chain dehydrogenase macD, with the help of macE, and a
CC       further prenylation by macG leads to 7-deacetoxyyanuthone A (By
CC       similarity). The next step is the hydroxylation of C-22 of 7-
CC       deacetoxyyanuthone A by the cytochrome P450 monooxygenase macH to yield
CC       22-deacetylyanuthone A (By similarity). O-Mevalon transferase macI then
CC       attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to
CC       produce yanuthone E (By similarity). The terpene cyclase macJ catalyzes
CC       the cyclization of 22-deacetylyanuthone A to macrophorin A
CC       (PubMed:28926261). MacJ is also able to catalyze cyclization of
CC       yanuthone E and 7-deacetoxyyanuthone A to their corresponding
CC       macrophorins (PubMed:28926261). The macJ products can be further
CC       modified by macH and macJ, as well as by the FAD-dependent
CC       monooxygenase macF, to produce additional macrophorins, including 4'-
CC       oxomacrophorin A, 4'-oxomacrophorin D and 4'-oxomacrophorin E
CC       (PubMed:28926261). {ECO:0000250|UniProtKB:G3Y421,
CC       ECO:0000269|PubMed:28926261}.
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}.
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DR   EMBL; MF990001; AVK70102.1; -; Genomic_DNA.
DR   EMBL; MH388470; QBC75446.1; -; Genomic_DNA.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR044851; Wax_synthase.
DR   InterPro; IPR032805; Wax_synthase_dom.
DR   PANTHER; PTHR31595; PTHR31595; 1.
DR   Pfam; PF13813; MBOAT_2; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..431
FT                   /note="O-Mevalon transferase macI"
FT                   /id="PRO_0000454090"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   431 AA;  47784 MW;  010CB663A367C14B CRC64;
     MAEMDVSSWK PTKLETKPFS LDSGHYTALA FVLAVCVPQA PHGTALRYGL LLLQITCGVQ
     AFLAQPPSVP DRAVLYTSGV LMGNLVARYF DRLYTTVPEK TFHRIIDSQT PEDTTQLSAP
     KRFFWALELF SVTRGIGWNW RVAGIPKSPV PITRFQFAAA QLLRWTVMYA GLHLVNVTCQ
     VVSSNPNAIP SLPGNLHIYA LIVCGFAITI YSHFAILMLP LSALCVGLQV GPRSWQAVAS
     WPPNFGSVRE AYSIRRFWGY TWHQQLRRQA GAPGAYLISL LPDSVMTSKR TAVKLARRYS
     LLMMSFVISG LIHACGTYQV TRALGLPLSD GGEMKYFALQ GMAIIAEDFG CWVLGIDDRG
     TQPGVMRRWM GYAITLSWYI WSRVQLKGVP VALAMGIEDE RGDLFAALEL VRVSAVAVPG
     NFVAMAWELI W