ID   JANA_PENJA              Reviewed;         349 AA.
AC   A0A0E3D8M3;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Terpene cyclase janA {ECO:0000250|UniProtKB:A0A455R4Z0};
DE            EC=5.4.99.- {ECO:0000250|UniProtKB:A0A455R4Z0};
DE   AltName: Full=Janthitremanes biosynthesis cluster protein A {ECO:0000303|PubMed:26213965};
GN   Name=janA {ECO:0000303|PubMed:26213965};
OS   Penicillium janthinellum (Penicillium vitale).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC   STRAIN=PN2408;
RX   PubMed=26213965; DOI=10.3390/toxins7082701;
RA   Nicholson M.J., Eaton C.J., Starkel C., Tapper B.A., Cox M.P., Scott B.;
RT   "Molecular cloning and functional analysis of gene clusters for the
RT   biosynthesis of indole-diterpenes in Penicillium crustosum and P.
RT   janthinellum.";
RL   Toxins 7:2701-2722(2015).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       the indole diterpenes janthitremanes such as shearinine K or shearinine
CC       A (PubMed:26213965). The geranylgeranyl diphosphate (GGPP) synthase
CC       janG catalyzes the first step in janthitremane biosynthesis via
CC       conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into
CC       geranylgeranyl pyrophosphate (GGPP) (PubMed:26213965). Condensation of
CC       indole-3-glycerol phosphate with GGPP by the prenyl transferase janC
CC       then forms 3-geranylgeranylindole (3-GGI) (PubMed:26213965).
CC       Epoxidation by the FAD-dependent monooxygenase janM leads to a
CC       epoxidized-GGI that is substrate of the terpene cyclase janB for
CC       cyclization to yield paspaline (PubMed:26213965). Paspaline is
CC       subsequently converted to 13-desoxypaspaline by the cytochrome P450
CC       monooxygenase janP, via beta-PC-M6 in a series of alpha-face oxidations
CC       (Probable). The cytochrome P450 monooxygenase janQ is proposed to carry
CC       out sequential beta-face oxidation steps at C-7 and C-13 of 13-
CC       desoxypaspaline to form paspalicine and paspalinine respectively
CC       (Probable). The indole diterpene prenyltransferase janD may then
CC       convert paspalinine into shearinine K which is substrate of janO and/or
CC       additional enzymes for oxidation and cyclization to generate shearinine
CC       A (Probable). {ECO:0000269|PubMed:26213965,
CC       ECO:0000305|PubMed:26213965}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:26213965}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the membrane-bound ascI terpene cyclase family.
CC       {ECO:0000305}.
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DR   EMBL; KF280651; AGZ20473.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3D8M3; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Glycoprotein; Isomerase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..349
FT                   /note="Terpene cyclase janA"
FT                   /id="PRO_5002410104"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   349 AA;  38226 MW;  CB5B4F9237FC0EA3 CRC64;
     MSQTTTAALI SLSVFAAYAK YYQSFQNGFI ALLSDMADTK SLSGLPGGLH CEYTGFAPLD
     RFLTACNIFF WPVFQGEVPN LSLYGVAFAS ALVPMWLVIV LETHRGRRPV AALMELAFLA
     GPLVQCLGPG LVIPAILSRL PMSTPGTKLP FGFDIGFYPS SMIIGYILPL ILAALPTPRV
     TAYEAKQQLI AVWQGWPVYT SLIMLIIHYL RPMRASQDWQ LKIACAFAFA CSTAGHLAFL
     WFARAKTASY HVFLPPIPWR ELQVASIEAG VLRFLQWDYT LSASAMLVWT VASYCRATGK
     RIGQSSSVIL IFGMAGVVFL GPCSVALLLY TSVALQRKGV TNYDCCRSS