ID   ANDD_EMEVA              Reviewed;         327 AA.
AC   A0A097ZPE3;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 1.
DT   03-AUG-2022, entry version 14.
DE   RecName: Full=Polyprenyl transferase andD {ECO:0000303|PubMed:25216349};
DE            EC=2.5.1.- {ECO:0000269|PubMed:25216349};
DE   AltName: Full=Anditomin synthesis protein D {ECO:0000303|PubMed:25216349};
GN   Name=andD {ECO:0000303|PubMed:25216349};
OS   Emericella variicolor (Aspergillus stellatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1549217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 12069 / CBS 136.55 / IMI 60316 / NBRC 32302;
RX   PubMed=25216349; DOI=10.1021/ja508127q;
RA   Matsuda Y., Wakimoto T., Mori T., Awakawa T., Abe I.;
RT   "Complete biosynthetic pathway of anditomin: nature's sophisticated
RT   synthetic route to a complex fungal meroterpenoid.";
RL   J. Am. Chem. Soc. 136:15326-15336(2014).
CC   -!- FUNCTION: Polyprenyl transferase; part of the gene cluster that
CC       mediates the biosynthesis of anditomin, a fungal meroterpenoid
CC       (PubMed:25216349). The first step of the pathway is the synthesis of
CC       3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase andM
CC       (PubMed:25216349). DMOA is then converted to the phthalide compound
CC       5,7-dihydroxy-4,6-dimethylphthalide (DHDMP) by the cytochrome P450
CC       monooxygenase andK, which is further prenylated by the
CC       prenyltransferase andD to yield farnesyl-DHDMP (PubMed:25216349).
CC       Further epoxidation by the FAD-dependent monooxygenase andE leads to
CC       epoxyfarnesyl-DHDMP (PubMed:25216349). The next step involves the
CC       terpene cyclase andB that converts epoxyfarnesyl-DHDMP into preandiloid
CC       A through opening of the epoxide ring followed by the cyclization of
CC       the farnesyl moiety (PubMed:25216349). Preandiloid A is in turn
CC       oxidized at the C-3 hydroxyl group to yield preandiloid B by the
CC       dehydrogenase andC (PubMed:25216349). The dioxygenase andA is solely
CC       responsible for the dehydrogenation of preandiloid B leading to the
CC       enone preandiloid C, as well as for the intriguing structural
CC       rearrangement to generate the bicyclo[2.2.2]octane core, transforming
CC       preandiloid C into andiconin (PubMed:25216349). FAD-binding
CC       monooxygenase andJ then produces andilesin D which is reduced by
CC       dehydrogenase andI to yield andilesin A (PubMed:25216349). Action of
CC       acetyltransferase andG followed by a spontaneous acetate elimination
CC       leads then to andilesin B, which is in turn substrate of the short
CC       chain dehydrogenase andH to yield andilesin C (PubMed:25216349).
CC       Finally, the dioxygenase andF catalyzes the transformation of andilesin
CC       C to anditomin (PubMed:25216349). {ECO:0000269|PubMed:25216349}.
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:25216349}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AB981314; BAP81858.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A097ZPE3; -.
DR   SMR; A0A097ZPE3; -.
DR   BioCyc; MetaCyc:MON-19043; -.
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   1: Evidence at protein level;
KW   Magnesium; Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..327
FT                   /note="Polyprenyl transferase andD"
FT                   /id="PRO_0000436580"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   327 AA;  36017 MW;  406BBD163352EACB CRC64;
     MSATTTEAKQ TFLCKERLPR RYHPPSKVLS RLPTSFLPYG ELLRLHKPLG YILVCYPFLV
     AGAFSASIAP EVLEADFWPR ITLLCLWSIF LRSGGCIWDD IADQHVDAKV ARTRLRPLPR
     GAVSNSQATI FAAGTFLCGF AFVAELPGVC MVDALIMLFF AVLYPYGKRH SNYPQLILGT
     IGWAIPMTMH GLNLRPLDHP IPMAAMFAFI ALVTIMNDII YARQDIEEDI KAGVGSMAVR
     FQHCLDALTF ALVFASSAAL VIAGKLGNMG APFFTISVGG HFGFFLFLAM ANQRDPKSGV
     EWAAKRCCTS ATFLLIVGMV VDLVWRS