ID   ATMD_ASPFL              Reviewed;         435 AA.
AC   A9JPE1;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Indole diterpene prenyltransferase atmD {ECO:0000303|PubMed:24038699};
DE            EC=2.5.1.- {ECO:0000269|PubMed:24038699, ECO:0000305|PubMed:19801473};
DE   AltName: Full=Aflatrem synthesis protein D {ECO:0000303|PubMed:19801473};
GN   Name=atmD {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).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=24038699; DOI=10.1128/aem.02496-13;
RA   Liu C., Minami A., Noike M., Toshima H., Oikawa H., Dairi T.;
RT   "Regiospecificities and prenylation mode specificities of the fungal indole
RT   diterpene prenyltransferases AtmD and PaxD.";
RL   Appl. Environ. Microbiol. 79:7298-7304(2013).
RN   [4]
RP   INDUCTION.
RX   PubMed=26686623; DOI=10.1016/j.micres.2015.08.007;
RA   Gilbert M.K., Mack B.M., Wei Q., Bland J.M., Bhatnagar D., Cary J.W.;
RT   "RNA sequencing of an nsdC mutant reveals global regulation of secondary
RT   metabolic gene clusters in Aspergillus flavus.";
RL   Microbiol. Res. 182:150-161(2016).
CC   -!- FUNCTION: Indole diterpene prenyltransferase; part of the ATM2 gene
CC       cluster that mediates the biosynthesis of aflatrem, a tremorgenic
CC       mycotoxin with acute neurotoxic effects (PubMed:19801473,
CC       PubMed:2867895). Synthesis of geranylgeranyl diphosphate (GGPP) by AtmG
CC       (a GGPP 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, PubMed:24038699).
CC       {ECO:0000269|PubMed:19801473, ECO:0000269|PubMed:24038699,
CC       ECO:0000269|PubMed:2867895}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=302 uM for dimethylallyl diphosphate (DMAPP)
CC         {ECO:0000269|PubMed:24038699};
CC         KM=131 uM for paspaline {ECO:0000269|PubMed:24038699};
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). Expression is
CC       regulated by nsdC (PubMed:26686623). {ECO:0000269|PubMed:19801473,
CC       ECO:0000269|PubMed:26686623}.
CC   -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AM921700; CAP53937.2; -; Genomic_DNA.
DR   AlphaFoldDB; A9JPE1; -.
DR   SMR; A9JPE1; -.
DR   VEuPathDB; FungiDB:AFLA_045490; -.
DR   VEuPathDB; FungiDB:F9C07_2281026; -.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR   CDD; cd13929; PT-DMATS_CymD; 1.
DR   InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR   InterPro; IPR012148; DMATS-type_fun.
DR   PANTHER; PTHR40627; PTHR40627; 1.
DR   Pfam; PF11991; Trp_DMAT; 1.
DR   PIRSF; PIRSF000509; Trp_DMAT; 1.
DR   TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE   1: Evidence at protein level;
KW   Transferase.
FT   CHAIN           1..435
FT                   /note="Indole diterpene prenyltransferase atmD"
FT                   /id="PRO_0000436128"
FT   BINDING         81..82
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         90
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         346
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         413
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ   SEQUENCE   435 AA;  49671 MW;  F1E4560E4E6C365B CRC64;
     MSTPKSDTCS PHQALARGMG FKNHHERLWW ATFGPLLEKL LALCNYPVSL QYQHLSFIYH
     HLLPYLGPYP TVENGFAWKT AYSPDGTPAE VSLNFDGPKK TVRMDHVPIS QWSGTPKDPF
     CQNVALELTK SLAGTLPDFT WDWFNHFVQT MFIPEPATDV VLAREPPNFR RMAMQSVNGC
     DLLTAGVRVK PVFNALWKSI ETGIPHDKLL FDSIRNNTEL FGAYLPALQV IEDYCQSDRA
     KEFQTRGCFL SFDATSIKDA RLKVYLHGPQ TAYMKVEDAF TLGGRLSNPN IQTGVKELRK
     LWYAVLNLPS DFPESEDLPA TDDLYQGWLV NYELRPNNPV PEPKVYIPVA INNKDQDSIV
     QGLQEFFDRH ESMDVRDYRD IFETLFLDAK NPTGIHHFIT FSYKAHPYVT CYYKPHLEPV
     PAKELEESDV KGLSK