ID   PAXB_PENPX              Reviewed;         243 AA.
AC   E3UBL6;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Terpene cyclase paxB {ECO:0000250|UniProtKB:Q0C8A7};
DE            EC=4.2.3.- {ECO:0000250|UniProtKB:Q0C8A7};
DE   AltName: Full=Paxilline synthesis protein B {ECO:0000303|PubMed:11169115};
GN   Name=paxB {ECO:0000303|PubMed:11169115};
OS   Penicillium paxilli.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=70109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=PN2013;
RX   PubMed=11169115; DOI=10.1046/j.1365-2958.2001.02265.x;
RA   Young C., McMillan L., Telfer E., Scott B.;
RT   "Molecular cloning and genetic analysis of an indole-diterpene gene cluster
RT   from Penicillium paxilli.";
RL   Mol. Microbiol. 39:754-764(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=PN2013;
RX   PubMed=23949005; DOI=10.3390/toxins5081422;
RA   Scott B., Young C.A., Saikia S., McMillan L.K., Monahan B.J., Koulman A.,
RA   Astin J., Eaton C.J., Bryant A., Wrenn R.E., Finch S.C., Tapper B.A.,
RA   Parker E.J., Jameson G.B.;
RT   "Deletion and gene expression analyses define the paxilline biosynthetic
RT   gene cluster in Penicillium paxilli.";
RL   Toxins 5:1422-1446(2013).
RN   [3]
RP   FUNCTION.
RX   PubMed=16494875; DOI=10.1016/j.febslet.2006.02.008;
RA   Saikia S., Parker E.J., Koulman A., Scott B.;
RT   "Four gene products are required for the fungal synthesis of the indole-
RT   diterpene, paspaline.";
RL   FEBS Lett. 580:1625-1630(2006).
CC   -!- FUNCTION: Terpene cyclase; part of the ATM2 gene cluster that mediates
CC       the biosynthesis of paxilline, a mycotoxin that acts as an inhibitor of
CC       mammalian maxi-K channels (PubMed:11169115, PubMed:23949005,
CC       PubMed:16494875). PaxG, the geranylgeranyl diphosphate (GGPP) synthase
CC       is proposed to catalyze the first step in paxilline biosynthesis
CC       (PubMed:23949005, PubMed:16494875). Condensation of indole-3-glycerol
CC       phosphate with GGPP by paxC then forms 3-geranylgeranylindole (3-GGI),
CC       followed by epoxidation and cyclization of this intermediate (by paxM
CC       and paxB) to form paspaline (PubMed:23949005, PubMed:16494875).
CC       Paspaline is subsequently converted to 13-desoxypaxilline by paxP, the
CC       latter being then converted to paxilline by paxQ (PubMed:23949005).
CC       Finally paxilline can be mono- and di-prenylated by paxD
CC       (PubMed:23949005). {ECO:0000269|PubMed:11169115,
CC       ECO:0000269|PubMed:16494875, ECO:0000269|PubMed:23949005}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:16494875, ECO:0000305|PubMed:11169115,
CC       ECO:0000305|PubMed:23949005}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the production of paxilline
CC       (PubMed:23949005). {ECO:0000269|PubMed:23949005}.
CC   -!- SIMILARITY: Belongs to the paxB family. {ECO:0000305}.
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DR   EMBL; HM171111; ADO29934.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3UBL6; -.
DR   BioCyc; MetaCyc:MON-18637; -.
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   Lyase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..243
FT                   /note="Terpene cyclase paxB"
FT                   /id="PRO_0000436122"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
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        134..154
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"
SQ   SEQUENCE   243 AA;  26917 MW;  5DC6CB8A4B41748E CRC64;
     MDGFDVSQAP PEYQAIKPLA DLFVVGMGVG WIINYIGMVY ISFKHETYGM SIMPLCCNIA
     WELVYCLVFP SKSPVERGVF WMGLLINFGV MYAAITFSSR EWGHAPLVER NISLIFFVAT
     MGFLSGHVAL ALEIGPALAY SWGAVICQLL LSVGGLSQLL CRGSTRGASY TLWASRFLGS
     TCTVGFAGLR WMYWSEAFGW LNSPLVLWSL VVFLSIDGFY GICFWYVDRN EKSLGISGPK
     KAN