ATMM_ASPFL
ID ATMM_ASPFL Reviewed; 479 AA.
AC Q672V4;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=FAD-dependent monooxygenase atmM {ECO:0000303|PubMed:15528556};
DE EC=1.-.-.- {ECO:0000305|PubMed:15528556, ECO:0000305|PubMed:19801473, ECO:0000305|PubMed:2867895};
DE AltName: Full=Aflatrem synthesis protein M {ECO:0000303|PubMed:15528556};
GN Name=atmM {ECO:0000303|PubMed:15528556};
GN ORFNames=AF113 {ECO:0000303|PubMed:15528556};
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], INDUCTION, AND FUNCTION.
RX PubMed=15528556; DOI=10.1128/aem.70.11.6875-6883.2004;
RA Zhang S., Monahan B.J., Tkacz J.S., Scott B.;
RT "Indole-diterpene gene cluster from Aspergillus flavus.";
RL Appl. Environ. Microbiol. 70:6875-6883(2004).
RN [2]
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 [3]
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 [4]
RP INDUCTION.
RX PubMed=16988822; DOI=10.1007/s00253-006-0581-5;
RA Duran R.M., Cary J.W., Calvo A.M.;
RT "Production of cyclopiazonic acid, aflatrem, and aflatoxin by Aspergillus
RT flavus is regulated by veA, a gene necessary for sclerotial formation.";
RL Appl. Microbiol. Biotechnol. 73:1158-1168(2007).
CC -!- FUNCTION: FAD-dependent monooxygenase; part of the ATM1 gene cluster
CC that mediates the biosynthesis of aflatrem, a tremorgenic mycotoxin
CC with acute neurotoxic effects (PubMed:15528556, 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).
CC {ECO:0000269|PubMed:15528556, ECO:0000269|PubMed:19801473,
CC ECO:0000269|PubMed:2867895}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
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 correlates with the onset of
CC aflatrem biosynthesis in stationary cultures (PubMed:15528556,
CC PubMed:19801473). Expression is induced by the developmental and
CC secondary metabolism regulator veA (PubMed:16988822).
CC {ECO:0000269|PubMed:15528556, ECO:0000269|PubMed:16988822,
CC ECO:0000269|PubMed:19801473}.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {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; AY559849; AAT65719.1; -; Genomic_DNA.
DR AlphaFoldDB; Q672V4; -.
DR SMR; Q672V4; -.
DR VEuPathDB; FungiDB:AFLA_096400; -.
DR VEuPathDB; FungiDB:F9C07_1723127; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Membrane; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..479
FT /note="FAD-dependent monooxygenase atmM"
FT /id="PRO_0000436118"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 37..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 319..323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 479 AA; 53877 MW; 61BC4A1AA452B7C1 CRC64;
MCDKDRFKVI IVGGSVAGLT LAHCLQRAGI DHVVLEKNSD LSPQVGASIG IIPNGGRILD
QLGLFDAVER MTYPLSIATI TYPDGYSFRN NYPKTVDERF GYPIAFLDRQ KFLEILHTSY
PDPSNIHTNC RVTHIRRHDS HMEVVTSSGQ EYTGDLVVGA DGVHSVIRSE MWKLADALEP
GRVSKREKRS MKVEYACVFG ISLPVPGLKV GDQVNAFHDG LTIITIHGKN GRVFWFVIKK
LDDMYTYPDT VRFSSADAVR TCENIVHFPL VNGATFGHVW ENREVTSMTA LEENIFNTWY
ADRIVCIGDS IHKMTPNIGQ GANTAIEDAT VLTNLLYDRL SKNGHKKLAR QELLQLLREF
QSQRFRRVNK IYQDSRFLVR LHARDGIVKS LLARYIVPYM TELPADLASK SIADSPTIGF
LPLPSRSGPG WLQWSRKQRR PATPWILVLL VIVVSFGLHS PELVIPTFWS NSLVSKTVE
