PAXM_PENPX
ID PAXM_PENPX Reviewed; 477 AA.
AC Q9C447;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=FAD-dependent monooxygenase paxM {ECO:0000303|PubMed:11169115};
DE EC=1.-.-.- {ECO:0000305|PubMed:11169115, ECO:0000305|PubMed:16494875, ECO:0000305|PubMed:23949005};
DE AltName: Full=Paxilline synthesis protein M {ECO:0000303|PubMed:11169115};
GN Name=paxM {ECO:0000303|PubMed:11169115};
OS Penicillium paxilli.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=70109 {ECO:0000312|EMBL:AAK11530.1};
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: FAD-dependent monooxygenase; 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, PubMed:16494875). PaxG, the geranylgeranyl diphosphate
CC (GGPP) synthase is proposed to catalyze the first step in paxilline
CC biosynthesis (PubMed:23949005, PubMed:16494875). Condensation of
CC indole-3-glycerol phosphate with GGPP by paxC then forms 3-
CC geranylgeranylindole (3-GGI), followed by epoxidation and cyclization
CC of this intermediate (by paxM and paxB) to form paspaline
CC (PubMed:23949005, PubMed:16494875). 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). {ECO:0000269|PubMed:11169115,
CC ECO:0000269|PubMed:16494875, ECO:0000269|PubMed:23949005}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:11169115, ECO:0000269|PubMed:16494875,
CC ECO:0000269|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 paxM FAD-dependent monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; HM171111; AAK11530.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9C447; -.
DR SMR; Q9C447; -.
DR BioCyc; MetaCyc:MON-18636; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Membrane; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..477
FT /note="FAD-dependent monooxygenase paxM"
FT /id="PRO_0000436119"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 36..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 131
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 318..322
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 477 AA; 53737 MW; 353B83810875BBD1 CRC64;
MEKAEFQVII VGGSIGGLTL AHCLHRAGIK HVVLEKASDP APQIGASIGI LPNGARVLDQ
LQLYDQVEEH IEPLSKATIG LPDGFNFSSS YPKIIDQRFG FPIAFLDRQK MLEILYKGYP
DPSKIRLGQR VTSIESLDDG VLITTTTGHV YRGDLLVGAD GVHSIVRREI WKARGIARRV
SKIKQDSSKL TVEFRCIFGI SSAMPGLKLG EQVNALFDGL TIVTIHGKDG RIYWFVIQKL
GKKYVYPDSP RYTSHETSIA AEEIRDVKFY ENITFGELWD KRETSSMTAL EENTFKVWHH
GRCVLLGDSV HKMTPNVGQG ANMAIEDAAA LANLLRKMRI SSGPYFPTSS QMEFLLQKYR
DLRYERVNTI YQSSRFLVRF QVRDGIIYSL LSRYWAPYAG DLPADMASKT IADGTMCDFL
PTPKRSGGGW EKYSKQGRSW SYLTQLMIYL FGLTIVYTSL TMMFDLEGAL KFYFLQV
