ID A9JPD3_ASPFL Unreviewed; 340 AA.
AC A9JPD3;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=(2E,6E)-farnesyl diphosphate synthase {ECO:0000256|ARBA:ARBA00032873};
DE EC=2.5.1.1 {ECO:0000256|ARBA:ARBA00012833};
DE EC=2.5.1.10 {ECO:0000256|ARBA:ARBA00012439};
DE EC=2.5.1.29 {ECO:0000256|ARBA:ARBA00012382};
DE AltName: Full=Dimethylallyltranstransferase {ECO:0000256|ARBA:ARBA00032448};
DE AltName: Full=Farnesyl diphosphate synthase {ECO:0000256|ARBA:ARBA00032424};
DE AltName: Full=Farnesyltranstransferase {ECO:0000256|ARBA:ARBA00032052};
DE AltName: Full=Geranylgeranyl diphosphate synthase {ECO:0000256|ARBA:ARBA00033096};
DE AltName: Full=Geranyltranstransferase {ECO:0000256|ARBA:ARBA00032380};
GN Name=atmG {ECO:0000313|EMBL:CAP47201.1};
OS Aspergillus flavus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5059 {ECO:0000313|EMBL:CAP47201.1};
RN [1] {ECO:0000313|EMBL:CAP47201.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 3357 {ECO:0000313|EMBL:CAP47201.1};
RX 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).
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:0000256|ARBA:ARBA00001744};
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:0000256|ARBA:ARBA00000028};
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:0000256|ARBA:ARBA00000969};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family.
CC {ECO:0000256|RuleBase:RU004466}.
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DR EMBL; AM911677; CAP47201.1; -; Genomic_DNA.
DR AlphaFoldDB; A9JPD3; -.
DR VEuPathDB; FungiDB:AFLA_000006; -.
DR VEuPathDB; FungiDB:F9C07_4242; -.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046165; P:alcohol biosynthetic process; IEA:UniProt.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:UniProt.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR PANTHER; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR12001:SF70; PYROPHOSPHATE SYNTHETASE ATMG, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G02400)-RELATED; 1.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR SUPFAM; SSF48576; Terpenoid synthases; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004466}.
FT REGION 19..50
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"
SQ SEQUENCE 340 AA; 38508 MW; 8153E038159A08B1 CRC64;
MISGVPDRWK LVASSLSSNL DASYPTPSSL STEPIDTRSS SPQGSASTEV DKEKIIRGPV
DYLLKCPGKD IRRKLMQAFN EWLKIPEDRL NIIAEIVGLL HTASLLIDDI QDSSKLRRGI
PVAHSIFGVA QTINSANYAY FAAQEKLREL NRPKAYEIFT EELLRLHRGQ GMDLYWRDSL
TCPTEEEYIE MISNKTGGLF RLAIKLMQLE SEVTSDFLGL VDLLGIIFQI RDDYQNLQSD
LYSKNKGFCE DLTEGKFSFL IIHSINSNLG NQQLLNILRQ RSEEESVKQY AVEYIRSTGS
FAYCQDRLAS LLHEAKMMVN VLEENVGFSK GIYDILAFLL
//
