ID   ANDL_EMEVA              Reviewed;         177 AA.
AC   A0A097ZPE6;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   07-JAN-2015, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Anditomin synthesis protein L {ECO:0000303|PubMed:25216349};
GN   Name=andL {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], AND FUNCTION.
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: Part of the gene cluster that mediates the biosynthesis of
CC       anditomin, a fungal meroterpenoid (PubMed:25216349). The first step of
CC       the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by
CC       the polyketide synthase andM (PubMed:25216349). DMOA is then converted
CC       to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHDMP)
CC       by the cytochrome P450 monooxygenase andK, which is further prenylated
CC       by the prenyltransferase andD to yield farnesyl-DHDMP
CC       (PubMed:25216349). Further epoxidation by the FAD-dependent
CC       monooxygenase andE leads to epoxyfarnesyl-DHDMP (PubMed:25216349). The
CC       next step involves the terpene cyclase andB that converts
CC       epoxyfarnesyl-DHDMP into preandiloid A through opening of the epoxide
CC       ring followed by the cyclization of the farnesyl moiety
CC       (PubMed:25216349). Preandiloid A is in turn oxidized at the C-3
CC       hydroxyl group to yield preandiloid B by the dehydrogenase andC
CC       (PubMed:25216349). The dioxygenase andA is solely responsible for the
CC       dehydrogenation of preandiloid B leading to the enone preandiloid C, as
CC       well as for the intriguing structural rearrangement to generate the
CC       bicyclo[2.2.2]octane core, transforming preandiloid C into andiconin
CC       (PubMed:25216349). FAD-binding monooxygenase andJ then produces
CC       andilesin D which is reduced by dehydrogenase andI to yield andilesin A
CC       (PubMed:25216349). Action of acetyltransferase andG followed by a
CC       spontaneous acetate elimination leads then to andilesin B, which is in
CC       turn substrate of the short chain dehydrogenase andH to yield andilesin
CC       C (PubMed:25216349). Finally, the dioxygenase andF catalyzes the
CC       transformation of andilesin C to anditomin (PubMed:25216349). The exact
CC       role of andL within the anditomin biosynthetic pathway has not been
CC       identified yet (PubMed:25216349). {ECO:0000269|PubMed:25216349}.
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}.
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DR   EMBL; AB981314; BAP81866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A097ZPE6; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1200.120; -; 1.
DR   InterPro; IPR037673; MSC/AndL.
DR   InterPro; IPR036019; MscL_channel.
DR   PANTHER; PTHR30266; PTHR30266; 1.
DR   Pfam; PF01741; MscL; 1.
DR   SUPFAM; SSF81330; SSF81330; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..177
FT                   /note="Anditomin synthesis protein L"
FT                   /id="PRO_0000436588"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   177 AA;  20014 MW;  62CD9470166D5F1F CRC64;
     MRGLGGSTET ALRLGSDAKD RVYRAWDGFI DFAARDNVLE VALGLIIAQA FTSVVNSFVS
     DIVLPLVSLL PFIMRNMDEK FAILSKGPHY QEGYNTIEQA RDDGALVLAY GVFLEKIVNF
     LGISLTLYTL AQLYMVFSKR KIIKRTVKCK YCRKWISERA LRCVNCSSWQ DGREDVQ