ID   ATMQ_ASPFL              Reviewed;         529 AA.
AC   A9JPE2;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Cytochrome P450 monooxygenase atmQ {ECO:0000303|PubMed:19801473};
DE            EC=1.-.-.- {ECO:0000305|PubMed:19801473};
DE   AltName: Full=Aflatrem synthesis protein Q {ECO:0000303|PubMed:19801473};
GN   Name=atmQ {ECO:0000303|PubMed:19801473};
OS   Aspergillus flavus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, INDUCTION, AND FUNCTION.
RC   STRAIN=NRRL 6541;
RX   PubMed=19801473; DOI=10.1128/aem.02146-08;
RA   Nicholson M.J., Koulman A., Monahan B.J., Pritchard B.L., Payne G.A.,
RA   Scott B.;
RT   "Identification of two aflatrem biosynthesis gene loci in Aspergillus
RT   flavus and metabolic engineering of Penicillium paxilli to elucidate their
RT   function.";
RL   Appl. Environ. Microbiol. 75:7469-7481(2009).
RN   [2]
RP   FUNCTION.
RX   PubMed=2867895; DOI=10.1289/ehp.8562459;
RA   Valdes J.J., Cameron J.E., Cole R.J.;
RT   "Aflatrem: a tremorgenic mycotoxin with acute neurotoxic effects.";
RL   Environ. Health Perspect. 62:459-463(1985).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the ATM2 gene cluster
CC       that mediates the biosynthesis of aflatrem, a tremorgenic mycotoxin
CC       with acute neurotoxic effects (PubMed:19801473, PubMed:2867895).
CC       Synthesis of geranylgeranyl diphosphate (GGPP) by AtmG (a GGPP
CC       synthase) precedes condensation of GGPP with indole 3-glycerol
CC       phosphate, followed by epoxidation and cyclization by AtmM (a FAD-
CC       dependent monooxygenase) and AtmC (a prenyltransferase) to produce
CC       paspaline (PubMed:19801473). AtmB is also essential for paspaline
CC       production, but its exact role has not been identified yet
CC       (PubMed:19801473). AtmP, a cytochrome P450 monooxygenase, subsequently
CC       converts paspaline to 13-desoxypaxilline via PC-M6 by removal of the C-
CC       30 methyl group and oxidation at C-10 (PubMed:19801473). AtmQ, a
CC       cytochrome P450 monooxygenase, then catalyzes the oxidation of 13-
CC       desoxypaxilline, first at C-7 to produce paspalicine and then at C-13
CC       to form paspalinine (PubMed:19801473). Finally, AtmD prenylates
CC       paspalinine to form aflatrem (PubMed:19801473).
CC       {ECO:0000269|PubMed:19801473, ECO:0000269|PubMed:2867895}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:19801473}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: The onset of expression occurs at 48 h old stationary
CC       cultures (PubMed:19801473). {ECO:0000269|PubMed:19801473}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AM921700; CAP53938.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9JPE2; -.
DR   SMR; A9JPE2; -.
DR   VEuPathDB; FungiDB:AFLA_045500; -.
DR   VEuPathDB; FungiDB:F9C07_2281027; -.
DR   BioCyc; MetaCyc:MON-18803; -.
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   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..529
FT                   /note="Cytochrome P450 monooxygenase atmQ"
FT                   /id="PRO_0000436126"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         467
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   529 AA;  61092 MW;  1DC8030DD7304ECD CRC64;
     MYRLLERTLD RFTGLVEYQP TYPFAAPTWV YLVGAILIQQ LATRWYRYYK SWVNVPVVGG
     HGIIGSWIAA FRWTARARSL VNEGYQKYGD FAFQVSTPTR WEVFICNDEM VREYRNFTDE
     RFSANALFEA KYTVPGAAEG VHKVPVPIVA KALTWQRTRA ATKTDPYFEE FVKELQHAFD
     AETKFENEDW NDLCCFATGT RIVAHLTAKS LVGYPLSRDT ELIDLFAEYG NAVPTSGFFI
     AMFPQILKPF AAKFCSAPKI SARLDRIVMD ELRKREANPR SEPQVQDITD WITFWSRTYP
     GTYTDQDIAR SVVSAVFGAI HTTTQVLVHC LTDLAIRPEY IHPLREEVET ILNRDDQQWT
     KEGLESMEKL DSFVKECQRF NPLDAGSLAR RATKDFTFSK GLHIPEGTFV FTPNSPVLFD
     EKHYPDAQQF DGYRFYRLGR VTGRPLEYKF IAANLKYLQF GDGRHICPGR FMAADEIRLL
     LAHILVNYDI RPKDDGERPP NWTFKKILFP DMKGMVQLKR RSINISQPN