PAXQ_PENPX
ID PAXQ_PENPX Reviewed; 512 AA.
AC Q9C450;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Cytochrome P450 monooxygenase paxQ {ECO:0000303|PubMed:12884010};
DE EC=1.-.-.- {ECO:0000305|PubMed:17428785};
DE AltName: Full=Paxilline synthesis protein Q {ECO:0000303|PubMed:11169115};
GN Name=paxQ {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, AND DISRUPTION PHENOTYPE.
RX PubMed=12884010; DOI=10.1007/s00438-003-0887-2;
RA McMillan L.K., Carr R.L., Young C.A., Astin J.W., Lowe R.G., Parker E.J.,
RA Jameson G.B., Finch S.C., Miles C.O., McManus O.B., Schmalhofer W.A.,
RA Garcia M.L., Kaczorowski G.J., Goetz M., Tkacz J.S., Scott B.;
RT "Molecular analysis of two cytochrome P450 monooxygenase genes required for
RT paxilline biosynthesis in Penicillium paxilli, and effects of paxilline
RT intermediates on mammalian maxi-K ion channels.";
RL Mol. Genet. Genomics 270:9-23(2003).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17428785; DOI=10.1074/jbc.m701626200;
RA Saikia S., Parker E.J., Koulman A., Scott B.;
RT "Defining paxilline biosynthesis in Penicillium paxilli: functional
RT characterization of two cytochrome P450 monooxygenases.";
RL J. Biol. Chem. 282:16829-16837(2007).
CC -!- FUNCTION: Cytochrome P450 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). 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, PubMed:17428785). Finally paxilline
CC can be mono- and di-prenylated by paxD (PubMed:23949005). PaxQ can also
CC utilized beta-paxitriol and alpha-PC-M6 as substrates converting them
CC to alpha-paxitriol (PubMed:17428785). {ECO:0000269|PubMed:11169115,
CC ECO:0000269|PubMed:12884010, ECO:0000269|PubMed:17428785,
CC ECO:0000269|PubMed:23949005}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:17428785, 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). Leads to the accumulation of the 13-desoxypaxillin
CC intermediate (PubMed:12884010). {ECO:0000269|PubMed:12884010,
CC ECO:0000269|PubMed:23949005}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; HM171111; AAK11527.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9C450; -.
DR SMR; Q9C450; -.
DR PRIDE; Q9C450; -.
DR KEGG; ag:AAK11527; -.
DR BioCyc; MetaCyc:MON-18639; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..512
FT /note="Cytochrome P450 monooxygenase paxQ"
FT /id="PRO_0000436127"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 453
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 512 AA; 58228 MW; 5693FD32A967C009 CRC64;
MDFVLSALQR DSWGIAAIIL VSIWALHSFH RSRKLQIPVP YVGKCGILGP WISALQWESK
ARELVQEGYE KHGNFAFKVA LLNRWEVCIC NEDMIREYKN LMDNQFSAIA VTSELFQIKW
TAPGTEEGAH KISIPLLGKA LTWQRNRSAA QNDPYFSEFV EEFLYAWKEE VPVPENGDYE
LPCFETGARV VAHLTARSLV GYPLCRNPEI VNLFTDYGSA VPTSGFFIAM FPEIMKPFVA
NFCSAPRISK RLQAILLEEF AKRREEGGIE STDIMGWLRN WTDQNEPGVY GDLEITSSII
ATIFGAIHTT TQVLVHCLFE LATRPEYVEP LRVEIQSALE EHGGWVKEGI EGMVKLDSFI
KECQRFNPLD AGSLARRATK DFTFKNGLTI PEGTFVFAPN GPILFDDTLY PEARQFDGYR
FYNLGQKTGK PQDFRFAATN QKYLQFGDGR HTCPGRWMAS DEIRLMLAHI LMNYDIATKD
NKGRPENWIF KKILFPDMKA VVILKARKSV SA
