PAXG_PENPX
ID PAXG_PENPX Reviewed; 371 AA.
AC Q9C446;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase paxG {ECO:0000250|UniProtKB:Q12051};
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=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};
DE AltName: Full=Paxilline synthesis protein G {ECO:0000303|PubMed:11169115};
GN Name=paxG {ECO:0000303|PubMed:11169115};
OS Penicillium paxilli.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=70109;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PN2013;
RX PubMed=11169115; DOI=10.1046/j.1365-2958.2001.02265.x;
RA Young C., McMillan L., Telfer E., Scott B.;
RT "Molecular cloning and genetic analysis of an indole-diterpene gene cluster
RT from Penicillium paxilli.";
RL Mol. Microbiol. 39:754-764(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PN2013;
RX PubMed=23949005; DOI=10.3390/toxins5081422;
RA Scott B., Young C.A., Saikia S., McMillan L.K., Monahan B.J., Koulman A.,
RA Astin J., Eaton C.J., Bryant A., Wrenn R.E., Finch S.C., Tapper B.A.,
RA Parker E.J., Jameson G.B.;
RT "Deletion and gene expression analyses define the paxilline biosynthetic
RT gene cluster in Penicillium paxilli.";
RL Toxins 5:1422-1446(2013).
RN [3]
RP FUNCTION.
RX PubMed=16494875; DOI=10.1016/j.febslet.2006.02.008;
RA Saikia S., Parker E.J., Koulman A., Scott B.;
RT "Four gene products are required for the fungal synthesis of the indole-
RT diterpene, paspaline.";
RL FEBS Lett. 580:1625-1630(2006).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND PEROXISOMAL TARGETING SIGNAL.
RX PubMed=19529962; DOI=10.1007/s00438-009-0463-5;
RA Saikia S., Scott B.;
RT "Functional analysis and subcellular localization of two geranylgeranyl
RT diphosphate synthases from Penicillium paxilli.";
RL Mol. Genet. Genomics 282:257-271(2009).
CC -!- FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene
CC cluster that mediates the biosynthesis of paxilline, a mycotoxin that
CC acts as an inhibitor of mammalian maxi-K channels (PubMed:11169115,
CC PubMed:23949005, PubMed:16494875, PubMed:19529962). PaxG, the
CC geranylgeranyl diphosphate (GGPP) synthase is proposed to catalyze the
CC first step in paxilline biosynthesis (PubMed:23949005, PubMed:16494875,
CC PubMed:19529962). Condensation of indole-3-glycerol phosphate with GGPP
CC by paxC then forms 3-geranylgeranylindole (3-GGI), followed by
CC epoxidation and cyclization of this intermediate (by paxM and paxB) to
CC form paspaline (PubMed:23949005, PubMed:16494875). Paspaline is
CC subsequently converted to 13-desoxypaxilline by paxP, the latter being
CC then converted to paxilline by paxQ (PubMed:23949005). Finally
CC paxilline can be mono- and di-prenylated by paxD (PubMed:23949005).
CC {ECO:0000269|PubMed:11169115, ECO:0000269|PubMed:16494875,
CC ECO:0000269|PubMed:19529962, ECO:0000269|PubMed:23949005}.
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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:16494875, ECO:0000269|PubMed:19529962,
CC ECO:0000305|PubMed:11169115, ECO:0000305|PubMed:23949005}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19529962}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of paxilline
CC (PubMed:11169115, PubMed:23949005). {ECO:0000269|PubMed:11169115,
CC ECO:0000269|PubMed:23949005}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {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; HM171111; AAK11531.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9C446; -.
DR SMR; Q9C446; -.
DR BioCyc; MetaCyc:MON-18634; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Peroxisome; Transferase.
FT CHAIN 1..371
FT /note="Geranylgeranyl pyrophosphate synthase paxG"
FT /id="PRO_0000436115"
FT MOTIF 369..371
FT /note="Peroxisomal targeting signal"
FT /evidence="ECO:0000269|PubMed:19529962"
FT BINDING 89
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 92
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 121
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 137
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 138
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 215
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 216
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 249
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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 BINDING 266
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 276
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT SITE 160
FT /note="Important for determining product chain length"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 371 AA; 42352 MW; 6A006DA633EC5A61 CRC64;
MSYILAEALN FVRRGISHLN YWGASHSLSA DNYWESNFQG FPRLLSDSSK APSTIRTVQV
LEDDVDDIAI QYNKIVRGPL DYLLAIPGKD IRSKLIDSFN IWLQLPEEKL SIVKDIINLL
HTASLLIDDI QDASRLRRGK PVAHDVYGVA QTINSANYAY YLQQARLKEI GDPRAFEIFT
RSLLDLHLGQ GMDLYWRDMV VCPTEEEYTR MVMYKTGGLF NLALDLMRIQ SRKNTDFSKL
VELLGVIFQI RDDYMNLQSG LYAEKKGLME DLTEGKFSYP IIHSIRASPE SSELLDILKQ
RTEDEAVKIR AVKIMESTGS FQYTRETLSR LSAEARGYVK KLETSLGPNP GIHKILDLLE
VEYPTNEKGR V
