GA6_GIBF5
ID GA6_GIBF5 Reviewed; 952 AA.
AC S0EA85;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Bifunctional ent-kaurene synthase {ECO:0000303|PubMed:10803977};
DE EC=4.2.3.19 {ECO:0000269|PubMed:10803977};
DE EC=5.5.1.13 {ECO:0000269|PubMed:10803977};
DE AltName: Full=CPS/KS {ECO:0000303|PubMed:9917370};
DE AltName: Full=Ent-copalyl diphosphate synthase {ECO:0000303|PubMed:9917370};
DE AltName: Full=Ent-kaur-16-ene synthase {ECO:0000250|UniProtKB:Q9UVY5};
DE AltName: Full=Gibberellin cluster-kaurene synthase {ECO:0000303|PubMed:23825955};
GN Name=CPS/KS {ECO:0000303|PubMed:9917370}; ORFNames=FFUJ_14336;
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, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
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, CATALYTIC ACTIVITY, AND PATHWAY.
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: Bifunctional ent-kaurene synthase; part of the gene cluster
CC that mediates the biosynthesis of gibberellins (GAs), diterpenoids that
CC may provide a selective advantage during infection of the preferred
CC host plant, rice (PubMed:23825955, PubMed:9917370, PubMed:10347043,
CC PubMed:12750377, PubMed:15925394). Gibberellins (GAs) are diterpenoids
CC and are synthesized via the mevalonate pathway (PubMed:12750377).
CC Biosynthesis of the major metabolite GA3 (gibberellic acid) from
CC geranylgeranyl diphosphate (GGPP) requires 13 steps (PubMed:12750377).
CC The GGPP produced by the geranylgeranyl diphosphate synthase GGS2 is
CC converted to ent-kaurene via ent-copalyldiphosphate in a two-step
CC cyclization reaction performed by the bifunctional ent-copalyl
CC diphosphate synthase/ent-kaurene synthase enzyme (CPS/KS)
CC (PubMed:9745028, PubMed:10803977, PubMed:12750377). Ent-Kaurene is
CC metabolized to GAs by a series of oxidation reactions catalyzed by
CC cytochrome P450 monooxygenases (PubMed:9917370, PubMed:12750377).
CC Cytochrome P450 monooxygenase P450-4 is an ent-kaurene oxidase that
CC catalyzes the three oxidation steps between ent-kaurene and ent-
CC kaurenoic acid (PubMed:11472927). The highly multifunctional cytochrome
CC P450 monooxygenase P450-1 then catalyzes four steps involving oxidation
CC at two carbon atoms, in the main pathway from ent-kaurenoic acid to
CC GA14 via GA12-aldehyde as well as producing kaurenolides and fujenoic
CC acids as by-products (PubMed:11320210). The cytochrome P450
CC monooxygenase P450-2 then converts GA14 to GA4 by removal of C-20
CC (PubMed:11943776). GA4 is further converted to GA7 by the GA4
CC 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=ent-copalyl diphosphate = diphosphate + ent-kaur-16-ene;
CC Xref=Rhea:RHEA:22220, ChEBI:CHEBI:15415, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58553; EC=4.2.3.19;
CC Evidence={ECO:0000269|PubMed:10803977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = ent-copalyl
CC diphosphate; Xref=Rhea:RHEA:14841, ChEBI:CHEBI:58553,
CC ChEBI:CHEBI:58756; EC=5.5.1.13;
CC Evidence={ECO:0000269|PubMed:10803977};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000269|PubMed:10803977, ECO:0000269|PubMed:9745028,
CC ECO:0000269|PubMed:9917370}.
CC -!- INDUCTION: Expression is induced under gibberellin-producing conditions
CC (PubMed:9917370). {ECO:0000269|PubMed:9917370}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of gibberellins
CC (PubMed:9917370). {ECO:0000269|PubMed:9917370}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; HF679027; CCT69398.1; -; Genomic_DNA.
DR AlphaFoldDB; S0EA85; -.
DR SMR; S0EA85; -.
DR STRING; 1279085.S0EA85; -.
DR EnsemblFungi; CCT69398; CCT69398; FFUJ_14336.
DR VEuPathDB; FungiDB:FFUJ_14336; -.
DR HOGENOM; CLU_005861_0_0_1; -.
DR BRENDA; 4.2.3.19; 2425.
DR UniPathway; UPA00390; -.
DR Proteomes; UP000016800; Chromosome 5.
DR GO; GO:0009905; F:ent-copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009899; F:ent-kaurene synthase 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 InterPro; IPR017057; Ent-kaurene_synthase_fun.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PIRSF; PIRSF036498; Ent-kaurene_synthase_fungi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 1: Evidence at protein level;
KW Isomerase; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..952
FT /note="Bifunctional ent-kaurene synthase"
FT /id="PRO_0000442046"
FT MOTIF 690..694
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:H8ZM73"
FT BINDING 690
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 690
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 694
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 694
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 848
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 952 AA; 106762 MW; E5E8C6D904C77A05 CRC64;
MPGKIENGTP KDLKTGNDFV SAAKSLLDRA FKSHHSYYGL CSTSCQVYDT AWVAMIPKTR
DNVKQWLFPE CFHYLLKTQA ADGSWGSLPT TQTAGILDTA SAVLALLCHA QEPLQILDVS
PDEMGLRIEH GVTSLKRQLA VWNDVEDTNH IGVEFIIPAL LSMLEKELDV PSFEFPCRSI
LERMHGEKLG HFDLEQVYGK PSSLLHSLEA FLGKLDFDRL SHHLYHGSMM ASPSSTAAYL
IGATKWDDEA EDYLRHVMRN GAGHGNGGIS GTFPTTHFEC SWIIATLLKG GFTLKQIDGD
GLRGLSTILL EALRDENGVI GFAPRTADVD DTAKALLALS LVNQPVSPDI MIKVFEGKDH
FTTFGSERDP SLTSNLHVLL SLLKQSNLSQ YHPQILKTTL FTCRWWWGSD HCVKDKWNLS
HLYPTMLLVE AFTEVLHLID GGELSSLFDE SFKCKIGLSI FQAVLRIILT QDNDGSWRGY
REQTCYAILA LVQARHVCFF THMVDRLQSC VDRGFSWLKS CSFHSQDLTW TSKTAYEVGF
VAEAYKLAAL QSASLEVPAA TIGHSVTSAV PSSDLEKYMR LVRKTALFSP LDEWGLMASI
IESSFFVPLL QAQRVEIYPR DNIKVDEDKY LSIIPFTWVG CNNRSRTFAS NRWLYDMMYL
SLLGYQTDEY MEAVAGPVFG DVSLLHQTID KVIDNTMGNL ARANGTVHSG NGHQHESPNI
GQVEDTLTRF TNSVLNHKDV LNSSSSDQDT LRREFRTFMH AHITQIEDNS RFSKQASSDA
FSSPEQSYFQ WVNSTGGSHV ACAYSFAFSN CLMSANLLQG KDAFPSGTQK YLISSVMRHA
TNMCRMYNDF GSIARDNAER NVNSIHFPEF TLCNGTSQNL DERKERLLKI ATYEQGYLDR
ALEALERQSR DDAGDRAGSK DMRKLKIVKL FCDVTDLYDQ LYVIKDLSSS MK
