ID   ATMP_ASPFL              Reviewed;         519 AA.
AC   A9JPE0;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Cytochrome P450 monooxygenase AtmP {ECO:0000303|PubMed:19801473};
DE            EC=1.-.-.- {ECO:0000305|PubMed:19801473};
DE   AltName: Full=Aflatrem synthesis protein P {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}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: The onset of expression occurs at 60 h old stationary
CC       cultures and the steady-state levels correlates with the onset of
CC       aflatrem biosynthesis at 108 h (PubMed:19801473).
CC       {ECO:0000269|PubMed:19801473}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM921700; CAP53941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9JPE0; -.
DR   SMR; A9JPE0; -.
DR   VEuPathDB; FungiDB:AFLA_045540; -.
DR   VEuPathDB; FungiDB:F9C07_5881; -.
DR   BioCyc; MetaCyc:MON-18805; -.
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   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..519
FT                   /note="Cytochrome P450 monooxygenase AtmP"
FT                   /id="PRO_0000436124"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         457
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   519 AA;  59046 MW;  D5E5382AC7BD24B2 CRC64;
     MDKLTATLAK VNYPSEVENG SMLLVVTLVI LFLWFIIPSP VKRSNVSVPT VTLFNPYLPE
     FLSRVWFNST AATVIYKGYR QHKDRAFRLL KPDGDIIVLS NKYVEELRQL PLTTLNALEA
     VFEDHVGKYT TILDDSHLHT EVIQKRLTPA INRLIPRIID ELDHGFAVEM PECEDKWVLI
     RPYEVFLRLV ARAGARVFVG PDFCRTEKWL TASIDFTKNI FMTITLLRPI PSFLHPIIGP
     MLPSSRSLDT QLRYVQDELL GPEIVKRRQR QASGDPDYEK PDDFLQWMID LAQNDKEGDP
     GNIAHRLLGL TSMAVVHTSA MSITHGLYDL ITMAQWLEPL RQEIQEAMPD WKSSSYSSLV
     SLRRLDSFLK ESQRFNPPGE LSFHRVVKKD LVLSDGLRLP KGTHICMASG PIGMDTKYVS
     DPTTFDAFRY VDGDKAQSQF VHTSATSMHF GLGRYACPGR FFATFVLKAI LSRFLVEYEF
     RFGPDQVGRP KNMLLGDKIV PNTSVDVYVR KRTGSRSTA