GA5_GIBF5
ID GA5_GIBF5 Reviewed; 393 AA.
AC S0E627;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase 2 {ECO:0000250|UniProtKB:Q12051};
DE Short=GGPP synthase 2 {ECO:0000305};
DE Short=GGPPSase 2 {ECO:0000305};
DE Short=GGS2 {ECO:0000303|PubMed:9917370};
DE EC=2.5.1.- {ECO:0000250|UniProtKB:Q12051};
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=Gibberellin cluster GGPP synthase {ECO:0000305};
GN Name=GGS2 {ECO:0000303|PubMed:9917370}; ORFNames=FFUJ_14335;
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
RN [2]
RP FUNCTION.
RX PubMed=9745028; DOI=10.1007/s002940050392;
RA Tudzynski B., Kawaide H., Kamiya Y.;
RT "Gibberellin biosynthesis in Gibberella fujikuroi: cloning and
RT characterization of the copalyl diphosphate synthase gene.";
RL Curr. Genet. 34:234-240(1998).
RN [3]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=9917370; DOI=10.1006/fgbi.1998.1095;
RA Tudzynski B., Hoelter K.;
RT "Gibberellin biosynthetic pathway in Gibberella fujikuroi: evidence for a
RT gene cluster.";
RL Fungal Genet. Biol. 25:157-170(1998).
RN [4]
RP FUNCTION.
RX PubMed=10347043; DOI=10.1128/aem.65.6.2558-2564.1999;
RA Linnemannstoens P., Voss T., Hedden P., Gaskin P., Tudzynski B.;
RT "Deletions in the gibberellin biosynthesis gene cluster of Gibberella
RT fujikuroi by restriction enzyme-mediated integration and conventional
RT transformation-mediated mutagenesis.";
RL Appl. Environ. Microbiol. 65:2558-2564(1999).
RN [5]
RP FUNCTION.
RX PubMed=10803977; DOI=10.1271/bbb.64.660;
RA Toyomasu T., Kawaide H., Ishizaki A., Shinoda S., Otsuka M., Mitsuhashi W.,
RA Sassa T.;
RT "Cloning of a full-length cDNA encoding ent-kaurene synthase from
RT Gibberella fujikuroi: functional analysis of a bifunctional diterpene
RT cyclase.";
RL Biosci. Biotechnol. Biochem. 64:660-664(2000).
RN [6]
RP FUNCTION.
RX PubMed=11472927; DOI=10.1128/aem.67.8.3514-3522.2001;
RA Tudzynski B., Hedden P., Carrera E., Gaskin P.;
RT "The P450-4 gene of Gibberella fujikuroi encodes ent-kaurene oxidase in the
RT gibberellin biosynthesis pathway.";
RL Appl. Environ. Microbiol. 67:3514-3522(2001).
RN [7]
RP FUNCTION.
RX PubMed=11320210; DOI=10.1073/pnas.091096298;
RA Rojas M.C., Hedden P., Gaskin P., Tudzynski B.;
RT "The P450-1 gene of Gibberella fujikuroi encodes a multifunctional enzyme
RT in gibberellin biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:5838-5843(2001).
RN [8]
RP FUNCTION.
RX PubMed=11943776; DOI=10.1074/jbc.m201651200;
RA Tudzynski B., Rojas M.C., Gaskin P., Hedden P.;
RT "The gibberellin 20-oxidase of Gibberella fujikuroi is a multifunctional
RT monooxygenase.";
RL J. Biol. Chem. 277:21246-21253(2002).
RN [9]
RP FUNCTION.
RX PubMed=12750377; DOI=10.1074/jbc.m301927200;
RA Tudzynski B., Mihlan M., Rojas M.C., Linnemannstons P., Gaskin P.,
RA Hedden P.;
RT "Characterization of the final two genes of the gibberellin biosynthesis
RT gene cluster of Gibberella fujikuroi: des and P450-3 encode GA4 desaturase
RT and the 13-hydroxylase, respectively.";
RL J. Biol. Chem. 278:28635-28643(2003).
RN [10]
RP FUNCTION.
RX PubMed=15925394; DOI=10.1016/j.phytochem.2005.04.012;
RA Malonek S., Boemke C., Bornberg-Bauer E., Rojas M.C., Hedden P.,
RA Hopkins P., Tudzynski B.;
RT "Distribution of gibberellin biosynthetic genes and gibberellin production
RT in the Gibberella fujikuroi species complex.";
RL Phytochemistry 66:1296-1311(2005).
CC -!- FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene
CC cluster that mediates the biosynthesis of gibberellins (GAs),
CC diterpenoids that may provide a selective advantage during infection of
CC the preferred host plant, rice (PubMed:23825955, PubMed:9917370,
CC PubMed:10347043, PubMed:12750377, PubMed:15925394). Gibberellins (GAs)
CC are diterpenoids and are synthesized via the mevalonate pathway
CC (PubMed:12750377). Biosynthesis of the major metabolite GA3
CC (gibberellic acid) from geranylgeranyl diphosphate (GGPP) requires 13
CC steps (PubMed:12750377). The GGPP produced by the geranylgeranyl
CC diphosphate synthase GGS2 is converted to ent-kaurene via ent-
CC copalyldiphosphate in a two-step cyclization reaction performed by the
CC bifunctional ent-copalyl diphosphate synthase/ent-kaurene synthase
CC enzyme (CPS/KS) (PubMed:9745028, PubMed:10803977, PubMed:12750377).
CC Ent-Kaurene is metabolized to GAs by a series of oxidation reactions
CC catalyzed by cytochrome P450 monooxygenases (PubMed:9917370,
CC PubMed:12750377). Cytochrome P450 monooxygenase P450-4 is an ent-
CC kaurene oxidase that catalyzes the three oxidation steps between ent-
CC kaurene and ent-kaurenoic acid (PubMed:11472927). The highly
CC multifunctional cytochrome P450 monooxygenase P450-1 then catalyzes
CC four steps involving oxidation at two carbon atoms, in the main pathway
CC from ent-kaurenoic acid to GA14 via GA12-aldehyde as well as producing
CC kaurenolides and fujenoic acids as by-products (PubMed:11320210). The
CC cytochrome P450 monooxygenase P450-2 then converts GA14 to GA4 by
CC removal of C-20 (PubMed:11943776). GA4 is further converted to GA7 by
CC the GA4 desaturase DES via 1,2-desaturation before cytochrome P450
CC monooxygenase P450-3, a 13-hydroxylase, hydroxylates GA7 to GA3, the
CC final product of the GA-biosynthetic pathway (PubMed:12750377).
CC {ECO:0000269|PubMed:10347043, ECO:0000269|PubMed:10803977,
CC ECO:0000269|PubMed:11320210, ECO:0000269|PubMed:11472927,
CC ECO:0000269|PubMed:11943776, ECO:0000269|PubMed:12750377,
CC ECO:0000269|PubMed:15925394, ECO:0000269|PubMed:23825955,
CC ECO:0000269|PubMed:9745028, ECO:0000269|PubMed:9917370}.
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: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000269|PubMed:9917370}.
CC -!- INDUCTION: Expression is induced under gibberellin-producing conditions
CC (PubMed:9917370). {ECO:0000269|PubMed:9917370}.
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; HF679027; CCT69172.1; -; Genomic_DNA.
DR AlphaFoldDB; S0E627; -.
DR SMR; S0E627; -.
DR STRING; 1279085.S0E627; -.
DR EnsemblFungi; CCT69172; CCT69172; FFUJ_14335.
DR VEuPathDB; FungiDB:FFUJ_14335; -.
DR HOGENOM; CLU_014015_6_0_1; -.
DR UniPathway; UPA00390; -.
DR Proteomes; UP000016800; Chromosome 5.
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:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..393
FT /note="Geranylgeranyl pyrophosphate synthase 2"
FT /id="PRO_0000442045"
FT BINDING 109
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 112
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 141
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 157
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 158
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 235
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
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 275
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 282
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 292
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 302
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 393 AA; 43836 MW; 93C2D17169F1065C CRC64;
MAEQQISNLL SMFDASHASQ KLEITVQMMD TYHYRETPPD SSSSEGGSLS RYDERRVSLP
LSHNAASPDI VSQLCFSTAM SSELNHRWKS QRLKVADSPY NYILTLPSKG IRGAFIDSLN
VWLEVPEDET SVIKEVIGML HNSSLIIDDF QDNSPLRRGK PSTHTVFGPA QAINTATYVI
VKAIEKIQDI VGHDALADVT GTITTIFQGQ AMDLWWTANA IVPSIQEYLL MVNDKTGALF
RLSLELLALN SEASISDSAL ESLSSAVSLL GQYFQIRDDY MNLIDNKYTD QKGFCEDLDE
GKYSLTLIHA LQTDSSDLLT NILSMRRVQG KLTAQQKMLV LEVMKTNGSL DWTSKLLGML
HTRVVAEIES LEVSTKRDNH ALRALVERLK LET
