ATMG_ASPFL
ID ATMG_ASPFL Reviewed; 340 AA.
AC Q672V6;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase atmG {ECO:0000303|PubMed:15528556};
DE Short=GGPP synthase {ECO:0000305};
DE Short=GGPPSase {ECO:0000305};
DE EC=2.5.1.- {ECO:0000305};
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000250|UniProtKB:Q12051};
DE AltName: Full=Aflatrem synthesis protein G {ECO:0000303|PubMed:15528556};
DE AltName: Full=Dimethylallyltranstransferase {ECO:0000250|UniProtKB:Q12051};
DE EC=2.5.1.1 {ECO:0000250|UniProtKB:Q12051};
DE AltName: Full=Farnesyl diphosphate synthase {ECO:0000250|UniProtKB:Q12051};
DE AltName: Full=Farnesyltranstransferase {ECO:0000250|UniProtKB:Q12051};
DE EC=2.5.1.29 {ECO:0000250|UniProtKB:Q12051};
DE AltName: Full=Geranylgeranyl diphosphate synthase {ECO:0000250|UniProtKB:Q12051};
DE AltName: Full=Geranyltranstransferase {ECO:0000250|UniProtKB:Q12051};
DE EC=2.5.1.10 {ECO:0000250|UniProtKB:Q12051};
GN Name=atmG {ECO:0000303|PubMed:15528556};
GN ORFNames=AF111 {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:AAT65717.1};
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).
CC -!- FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the ATM1 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).
CC {ECO:0000269|PubMed:19801473, ECO:0000269|PubMed:2867895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-
CC geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:128769; EC=2.5.1.1;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:175763; EC=2.5.1.10;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};
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 FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AY559849; AAT65717.1; -; Genomic_DNA.
DR AlphaFoldDB; Q672V6; -.
DR SMR; Q672V6; -.
DR VEuPathDB; FungiDB:AFLA_105050; -.
DR VEuPathDB; FungiDB:F9C07_4242; -.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 2: Evidence at transcript level;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..340
FT /note="Geranylgeranyl pyrophosphate synthase atmG"
FT /id="PRO_0000436114"
FT REGION 19..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 72
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 101
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
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="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 118
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 195
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 196
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 229
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 236
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 246
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 256
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT SITE 140
FT /note="Important for determining product chain length"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 340 AA; 38470 MW; ED0A5D097AD00043 CRC64;
MISGVPDRWK VVASSLSSNL DASYPTSSSL STEPIDTRSS SPQGSASTPV DKEKIIRGPV
DYLLKCPGKD IRRKLMQAFN EWLRIPEDRL NIIAEIVGLL HTASLLIDDI QDSSKLRRGI
PVAHSIFGVA QTINSANYAY FAAQEKLREL NRPKAYEIFT EELLRLHRGQ GMDLYWRDSL
TCPTEEEYIE MISNKTGGLF RLAIKLMQLE SEVTSDFLGL VDLLGVIFQI RDDYQNLQSD
LYSKNKGFCE DLTEGKFSFL IIHSINSNPG NQQLLNILRQ RSEEESVKKY AVEYIRSTGS
FAYCQDRLAS FLHEAKMMVN VLEDNVGFSK GIYDILAFLL
