ID   ATMA_ASPFL              Reviewed;         366 AA.
AC   A9JPE4;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Terpene cyclase atmA {ECO:0000250|UniProtKB:A0A455R4Z0};
DE            EC=5.4.99.- {ECO:0000250|UniProtKB:A0A455R4Z0};
DE   AltName: Full=Aflatrem synthesis protein A {ECO:0000303|PubMed:19801473};
GN   Name=atmA {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: Aflatrem synethesis protein A; 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). The role of atmA in the
CC       aflatrem biosynthesis is still unknown (PubMed:19801473).
CC       {ECO:0000269|PubMed:19801473, ECO:0000269|PubMed:2867895}.
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 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 membrane-bound ascI terpene cyclase family.
CC       {ECO:0000305}.
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DR   EMBL; AM921700; CAP53940.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9JPE4; -.
DR   VEuPathDB; FungiDB:AFLA_045520; -.
DR   VEuPathDB; FungiDB:AFLA_045530; -.
DR   VEuPathDB; FungiDB:F9C07_1872228; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Isomerase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..366
FT                   /note="Terpene cyclase atmA"
FT                   /id="PRO_0000436120"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   366 AA;  40985 MW;  D57459A7367927C2 CRC64;
     MDSVLRYVFL LLAMTSFYMM YISLFNNGFF NLLSHQLATR ALPGESDIAL LSEYTGLKAF
     DGILESIVIF FWPISQGHHV GLSLTGLSFS GGMVGIWMIV VVHICRIRSF TRGMVITLIV
     GIAQQAVGPG IVIPCYFALT SRARPPNKNL HLTGTYSTSN HGLVVSMIMS YIFPLVIMSL
     PAPAMISPHS KQQVIAAWQG WPVYFVIIMT THHLFINRGH RKEASARRQV LSVYHFGFAC
     SCLCHMAWLS AFVASKIQSL SQSSNFWYLC PYGVAFPLLN QPAQRLGALE AGLFTFLQWD
     YCVAAAATMV WSTDRYIQEC HRAELEIDKF RLILRLLGWI LIDGPSATAV RLIWESEGPS
     YLQNPN