GGS_NEOBT
ID GGS_NEOBT Reviewed; 343 AA.
AC Q6F5E6;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase {ECO:0000250|UniProtKB:Q12051};
DE Short=GGPP synthase {ECO:0000305};
DE Short=GGPPSase {ECO:0000305};
DE EC=2.5.1.- {ECO:0000269|PubMed:21897020};
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:0000303|PubMed:14745177};
DE AltName: Full=Geranyltranstransferase {ECO:0000250|UniProtKB:Q12051};
DE EC=2.5.1.10 {ECO:0000250|UniProtKB:Q12051};
GN Name=GGS;
OS Neocamarosporium betae (Beet black rot fungus) (Pleospora betae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Neocamarosporium.
OX NCBI_TaxID=1979465;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION OF GENE CLUSTER.
RC STRAIN=PS-16;
RX PubMed=14745177; DOI=10.1271/bbb.68.146;
RA Toyomasu T., Nakaminami K., Toshima H., Mie T., Watanabe K., Ito H.,
RA Matsui H., Mitsuhashi W., Sassa T., Oikawa H.;
RT "Cloning of a gene cluster responsible for the biosynthesis of diterpene
RT aphidicolin, a specific inhibitor of DNA polymerase alpha.";
RL Biosci. Biotechnol. Biochem. 68:146-152(2004).
RN [2]
RP FUNCTION.
RX PubMed=11457369; DOI=10.1021/ja015747j;
RA Oikawa H., Toyomasu T., Toshima H., Ohashi S., Kawaide H., Kamiya Y.,
RA Ohtsuka M., Shinoda S., Mitsuhashi W., Sassa T.;
RT "Cloning and functional expression of cDNA encoding aphidicolan-16 beta-ol
RT synthase: a key enzyme responsible for formation of an unusual diterpene
RT skeleton in biosynthesis of aphidicolin.";
RL J. Am. Chem. Soc. 123:5154-5155(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=21897020; DOI=10.1271/bbb.110366;
RA Fujii R., Minami A., Tsukagoshi T., Sato N., Sahara T., Ohgiya S., Gomi K.,
RA Oikawa H.;
RT "Total biosynthesis of diterpene aphidicolin, a specific inhibitor of DNA
RT polymerase alpha: heterologous expression of four biosynthetic genes in
RT Aspergillus oryzae.";
RL Biosci. Biotechnol. Biochem. 75:1813-1817(2011).
CC -!- FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene
CC cluster that mediates the biosynthesis of aphidicolin, a specific
CC inhibitor of eukaryotic DNA synthesis and DNA polymerase alpha
CC (PubMed:14745177, PubMed:21897020). The geranylgeranyl pyrophosphate
CC synthase GGS is required for supplying a sufficient amount of
CC geranylgeranyl diphosphate (GGDP), the general precursor of diterpenes
CC (PubMed:21897020). The diterpene synthase ACS then catalyzes the
CC conversion of geranylgeranyl diphosphate to aphidicolan-16-beta-ol via
CC the intermediate syn-copalyldiphosphate (syn-CDP) (PubMed:11457369,
CC PubMed:21897020). In addition to aphidicolan-16-beta-ol, the enzyme
CC produces also low levels of amphidicol-15-ene and amphidicol-16-ene
CC (PubMed:11457369). The cytochrome P450 monooxygenase P450-2 then
CC catalyzes the two-step hydroxylation from aphidicolan-16-beta-ol to 3-
CC deoxyaphidicolin via a 17,3-deoxyaphidicolin intermediate
CC (PubMed:21897020). Finally, the cytochrome P450 monooxygenase P450-1
CC converts 3-deoxyaphidicolin to aphidicolin (PubMed:21897020).
CC {ECO:0000269|PubMed:11457369, ECO:0000269|PubMed:14745177,
CC ECO:0000269|PubMed:21897020}.
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: Mycotoxin biosynthesis. {ECO:0000269|PubMed:21897020}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AB114137; BAD29970.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6F5E6; -.
DR SMR; Q6F5E6; -.
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:InterPro.
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.
PE 1: Evidence at protein level;
KW Magnesium; Metal-binding; Transferase.
FT CHAIN 1..343
FT /note="Geranylgeranyl pyrophosphate synthase"
FT /id="PRO_0000438560"
FT REGION 1..26
FT /note="Disordered"
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 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 343 AA; 39009 MW; E542DFF35017CD73 CRC64;
MAYTVEPREH SKNTTLPTVA MPPSPPSSFS ASFGPFRYDT KEVNFDHWTS TKEKVVTGPY
DYIAAKPGKE VRTLLLACFD EWLQVPPESL EVIGQVVRML HTASLLIDDI QDNSELRRGK
PVAQNIFGTA LTINSANYVY FLALEKLNSL KNPNITDIFT EELLRLHRGQ AMDLYWRDTL
TCPTEEEYFE MVANMTGGLF WLMYRMMNAE SSMPIDLLPV VELLGVIFQV LDDYKNLCSR
EYGKLKGFGE DLTEGKFSFP VIHSIRSNPE DLQLLHVLQQ KSSNEHVKLY AIEIMESTGS
LEYTKHVVEN IVSQIQEIIY STDEGQGRGK GILDLLHKIT RLS
