ID   PENB_PENCR              Reviewed;         243 AA.
AC   A0A0E3D8M2;
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 penB {ECO:0000303|PubMed:26213965};
DE            EC=4.2.3.- {ECO:0000305|PubMed:26213965};
DE   AltName: Full=Penitrem biosynthesis cluster protein B {ECO:0000303|PubMed:26213965};
GN   Name=penB;
OS   Penicillium crustosum (Blue mold fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=36656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC   STRAIN=PN2402;
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: Terpene cyclase; part of the gene cluster that mediates the
CC       biosynthesis of the indole diterpenes penitrems (PubMed:26213965). The
CC       geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first
CC       step in penitrem biosynthesis via conversion of farnesyl pyrophosphate
CC       and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP)
CC       (Probable). Condensation of indole-3-glycerol phosphate with GGPP by
CC       the prenyl transferase penC then forms 3-geranylgeranylindole (3-GGI)
CC       (Probable). Epoxidation by the FAD-dependent monooxygenase penM leads
CC       to a epoxidized-GGI that is substrate of the terpene cyclase penB for
CC       cyclization to yield paspaline (Probable). Paspaline is subsequently
CC       converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase
CC       penP, the latter being then converted to paxilline by the cytochrome
CC       P450 monooxygenase penQ (PubMed:26213965). Paxilline is converted to
CC       beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase
CC       PC-15 which can be monoprenylated at the C-20 by the indole diterpene
CC       prenyltransferase penD (Probable). A two-step elimination (acetylation
CC       and elimination) process performed by the O-acetyltransferase PC-16 and
CC       the P.simplicissimum ptmI-ortholog not yet identified in P.crustosum,
CC       leads to the production of the prenylated form of penijanthine
CC       (Probable). The FAD-linked oxidoreductase ptmO then converts the
CC       prenylated form of penijanthine into PC-M5 which is in turn transformed
CC       into PC-M4 by the aromatic dimethylallyltransferase PC-22 (Probable). A
CC       series of oxidation steps involving 4 cytochrome P450 monooxygenases
CC       (PC-21, PC-05, PC-23, PC-20) and a FAD-dependent monooxygenase (PC-14)
CC       are required for the transformation of PC-M4 to penitrems A and E.
CC       Synthesis of these final products is proposed to proceed via penitrems
CC       D and C (PC-21, PC-05, PC-14) and penitrems B and F (PC-21, PC-05, PC-
CC       14, PC-23) (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 paxB family. {ECO:0000305}.
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DR   EMBL; KC963408; AGZ20190.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3D8M2; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR039020; PaxB-like.
DR   PANTHER; PTHR42038; PTHR42038; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Lyase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..243
FT                   /note="Terpene cyclase penB"
FT                   /id="PRO_0000446545"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   243 AA;  27116 MW;  C2D595052095911B CRC64;
     MDGFDVSQAP PEYRAVEPIA NIFVLGMGLG WLINYVGMIY QSFKDETYGM AIMPLCCNIA
     WEIVYSLIYP SKSLIEQGVF IAGLTINIGV MYAAIKFAPK EWSHAPLVMR NLSLIFFLAT
     LGFLTGHLAL AAEIGHSLAY SWGAVVCQLL LSVGGLCQLL CRGSTRGASY TLWLSRFLGS
     SCTVAFASLR WMYWPESFSW LNSPLVLWSL ALFLTVDGSY GLCYWYVRQY ELSLKEAEGR
     KSK