ID   ATMB_ASPFL              Reviewed;         243 AA.
AC   A9JPE3;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Terpene cyclase atmB {ECO:0000250|UniProtKB:Q0C8A7};
DE            EC=4.2.3.- {ECO:0000250|UniProtKB:Q0C8A7};
DE   AltName: Full=Aflatrem synthesis protein B {ECO:0000303|PubMed:19801473};
GN   Name=atmB {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   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: Terpene cyclase; part of the ATM2 gene cluster that mediates
CC       the biosynthesis of aflatrem, a tremorgenic mycotoxin with acute
CC       neurotoxic effects (PubMed:19801473, PubMed:2867895). Synthesis of
CC       geranylgeranyl diphosphate (GGPP) by AtmG (a GGPP synthase) precedes
CC       condensation of GGPP with indole 3-glycerol phosphate, followed by
CC       epoxidation and cyclization by AtmM (a FAD-dependent monooxygenase) and
CC       AtmC (a prenyltransferase) to produce paspaline (PubMed:19801473). AtmB
CC       is also essential for paspaline production, but its exact role has not
CC       been identified yet (PubMed:19801473). AtmP, a cytochrome P450
CC       monooxygenase, subsequently converts paspaline to 13-desoxypaxilline
CC       via PC-M6 by removal of the C-30 methyl group and oxidation at C-10
CC       (PubMed:19801473). AtmQ, a cytochrome P450 monooxygenase, then
CC       catalyzes the oxidation of 13-desoxypaxilline, first at C-7 to produce
CC       paspalicine and then at C-13 to form paspalinine (PubMed:19801473).
CC       Finally, AtmD prenylates paspalinine to form aflatrem
CC       (PubMed:19801473). {ECO:0000269|PubMed:19801473,
CC       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). Expression is
CC       regulated by nsdC (PubMed:26686623). {ECO:0000269|PubMed:19801473,
CC       ECO:0000269|PubMed:26686623}.
CC   -!- SIMILARITY: Belongs to the paxB family. {ECO:0000305}.
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DR   EMBL; AM921700; CAP53939.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9JPE3; -.
DR   VEuPathDB; FungiDB:AFLA_045510; -.
DR   VEuPathDB; FungiDB:F9C07_5878; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR039020; PaxB-like.
DR   PANTHER; PTHR42038; PTHR42038; 1.
PE   2: Evidence at transcript level;
KW   Lyase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..243
FT                   /note="Terpene cyclase atmB"
FT                   /id="PRO_0000436121"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   243 AA;  27162 MW;  61FE681DC85EDD4D CRC64;
     MDGFGSSQAP AAYREVEWIA DVFVIGMGIG WIINYVGMVY GSLKGRTYGM AIMPLCCNIA
     WEIVYGLIYP SKTLYEQGVF LSGLTINLGV IYTAIKFGPK EWTHAPLVMH NLPLIFMLGI
     LGFLTGHLAL AAEIGPALAY NWGAAFCQLL LSVGGLCQLI SRGSTRGASY TLWLSRFLGS
     FSVVISAWLR YKYWPQAFSW LGKPLILWCL FAWLVVDGSY GVCFYYVKRY ERRIGHDSDR
     KTV