ATMC_ASPFL
ID ATMC_ASPFL Reviewed; 334 AA.
AC Q672V5;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Prenyl transferase atmC {ECO:0000303|PubMed:15528556};
DE EC=2.5.1.- {ECO:0000305};
DE AltName: Full=Aflatrem synthesis protein C {ECO:0000303|PubMed:15528556};
GN Name=atmC {ECO:0000303|PubMed:15528556};
GN ORFNames=AF112 {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 {ECO:0000312|EMBL:AAT65718.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
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).
RN [5]
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: Prenyl transferase; part of the ATM1 gene cluster that
CC mediates the biosynthesis of aflatrem, a tremorgenic mycotoxin with
CC acute neurotoxic effects (PubMed:19801473, PubMed:2867895). Synthesis
CC of 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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:19801473, ECO:0000305|PubMed:2867895}.
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). Expression is
CC also regulated by nsdC (PubMed:26686623). {ECO:0000269|PubMed:15528556,
CC ECO:0000269|PubMed:16988822, ECO:0000269|PubMed:19801473,
CC ECO:0000269|PubMed:26686623}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AY559849; AAT65718.1; -; Genomic_DNA.
DR AlphaFoldDB; Q672V5; -.
DR SMR; Q672V5; -.
DR VEuPathDB; FungiDB:AFLA_096390; -.
DR VEuPathDB; FungiDB:F9C07_9323; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 2: Evidence at transcript level;
KW Magnesium; Metal-binding; Transferase.
FT CHAIN 1..334
FT /note="Prenyl transferase atmC"
FT /id="PRO_0000436116"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 334 AA; 38068 MW; 632597B772EC150E CRC64;
MGFFHDFLSR PTTYAILAVL VIPVTALAWD RLPPLLPSAK RLLVGKKNPS KITSLECPYS
YIRQIYGTHH WAPFVDKLSP SLKTERPAKY HMILEIMDGI HLCLMLVDDI SDGSDYRKGR
PAAHHIYGPS ETANRAYYRV TQLLNRTGHE FPELAPWLLQ CLEEILEGQD LSLVWRRDGL
SAFPVQPEER VAAYRQMAYL KTGALFRLVG QLVLENQSYD DTLSTVAWYS QLQNDCKNVY
SSDYAKAKGA IAEDLRNGEL SYPIVVALNV PKGQYVVPAL EFRSPHNIRQ ALRVIQSDQV
RNICLTEMKK SAVSIQDWLA LWGRNEKMDM KSEK
