ID   PAXA_PENPX              Reviewed;         356 AA.
AC   E3UBL5;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Terpene cyclase paxA {ECO:0000250|UniProtKB:A0A455R4Z0};
DE            EC=5.4.99.- {ECO:0000250|UniProtKB:A0A455R4Z0};
DE   AltName: Full=Paxilline synthesis protein A {ECO:0000303|PubMed:11169115};
DE   Flags: Precursor;
GN   Name=paxA {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).
CC   -!- FUNCTION: Paxilline synthesis protein A: Part of the gene cluster that
CC       mediates the biosynthesis of paxilline, a mycotoxin that acts as an
CC       inhibitor of mammalian maxi-K channels (PubMed:11169115,
CC       PubMed:23949005). PaxG, the geranylgeranyl diphosphate (GGPP) synthase
CC       is proposed to catalyze the first step in paxilline biosynthesis
CC       (PubMed:23949005). Condensation of indole-3-glycerol phosphate with
CC       GGPP by paxC then forms 3-geranylgeranylindole (3-GGI), followed by
CC       epoxidation and cyclization of this intermediate (by paxM and paxB) to
CC       form paspaline (PubMed:23949005). Paspaline is subsequently converted
CC       to 13-desoxypaxilline by paxP, the latter being then converted to
CC       paxilline by paxQ (PubMed:23949005). Finally paxilline can be mono- and
CC       di-prenylated by paxD (PubMed:23949005). The exact role of paxA in
CC       paxilline biosynthesis is still unknown (PubMed:23949005).
CC       {ECO:0000269|PubMed:11169115, ECO:0000269|PubMed:23949005}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:11169115, 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 membrane-bound ascI terpene cyclase family.
CC       {ECO:0000305}.
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DR   EMBL; HM171111; ADO29933.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3UBL5; -.
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   Isomerase; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..356
FT                   /note="Terpene cyclase paxA"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003182478"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   356 AA;  39816 MW;  45742BC0E8F2C1DA CRC64;
     MTSITTSVLV LHSLLAANFK YYQSFQNGFI DMLSAMADSN SVSGLPGQLC REYTGIRPLD
     TFLTSCTVFF WPTFQGEIPG LSLYGIAFAS AMIPMWLIIV IDVHRRRQPF GALVELIAFA
     GPLIQCIGPG LVMPLLLARI HTPSRDSKSA SQFDYRTFIP SMIIGYILPL LLASLPAPLI
     LSYHNKQQFI AIWQGWPLYS SVLMWAFRRR SGHVHCSRHK GLKHACIFAL ACSSAGHLVL
     LSLTWLWSLS YWGYIQSAPW NEPPLASLEA GVLRFLQWDY TLSASATLSW AIAFRHEVVQ
     QKSLRISLLS LLRCLIGIVF LGPCSMVALL YWQTCSLQEE AGQKAPAKDK QLDQEI