S0EA85 · GA6_GIBF5

Function

function

Bifunctional ent-kaurene synthase; part of the gene cluster that mediates the biosynthesis of gibberellins (GAs), diterpenoids that may provide a selective advantage during infection of the preferred host plant, rice (PubMed:10347043, PubMed:12750377, PubMed:15925394, PubMed:23825955, PubMed:9917370).
Gibberellins (GAs) are diterpenoids and are synthesized via the mevalonate pathway (PubMed:12750377).
Biosynthesis of the major metabolite GA3 (gibberellic acid) from geranylgeranyl diphosphate (GGPP) requires 13 steps (PubMed:12750377).
The GGPP produced by the geranylgeranyl diphosphate synthase GGS2 is converted to ent-kaurene via ent-copalyldiphosphate in a two-step cyclization reaction performed by the bifunctional ent-copalyl diphosphate synthase/ent-kaurene synthase enzyme (CPS/KS) (PubMed:10803977, PubMed:12750377, PubMed:9745028).
Ent-Kaurene is metabolized to GAs by a series of oxidation reactions catalyzed by cytochrome P450 monooxygenases (PubMed:12750377, PubMed:9917370).
Cytochrome P450 monooxygenase P450-4 is an ent-kaurene oxidase that catalyzes the three oxidation steps between ent-kaurene and ent-kaurenoic acid (PubMed:11472927).
The highly multifunctional cytochrome P450 monooxygenase P450-1 then catalyzes four steps involving oxidation at two carbon atoms, in the main pathway from ent-kaurenoic acid to GA14 via GA12-aldehyde as well as producing kaurenolides and fujenoic acids as by-products (PubMed:11320210).
The cytochrome P450 monooxygenase P450-2 then converts GA14 to GA4 by removal of C-20 (PubMed:11943776).
GA4 is further converted to GA7 by the GA4 desaturase DES via 1,2-desaturation before cytochrome P450 monooxygenase P450-3, a 13-hydroxylase, hydroxylates GA7 to GA3, the final product of the GA-biosynthetic pathway (PubMed:12750377).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 3 Mg2+ ions per subunit.

Pathway

Plant hormone biosynthesis; gibberellin biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site690Mg2+ 1 (UniProtKB | ChEBI)
Binding site690Mg2+ 2 (UniProtKB | ChEBI)
Binding site694Mg2+ 1 (UniProtKB | ChEBI)
Binding site694Mg2+ 2 (UniProtKB | ChEBI)
Binding site848Mg2+ 3 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionent-copalyl diphosphate synthase activity
Molecular Functionent-kaurene synthase activity
Molecular Functionmagnesium ion binding
Biological Processgibberellin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional ent-kaurene synthase
  • EC number
  • Alternative names
    • CPS/KS
    • Ent-copalyl diphosphate synthase
    • Ent-kaur-16-ene synthase
    • Gibberellin cluster-kaurene synthase

Gene names

    • Name
      CPS/KS
    • ORF names
      FFUJ_14336

Organism names

Accessions

  • Primary accession
    S0EA85

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Impairs the production of gibberellins (PubMed:9917370).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004420461-952Bifunctional ent-kaurene synthase

Expression

Induction

Expression is induced under gibberellin-producing conditions (PubMed:9917370).

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif690-694DDXXD motif

Domain

The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg2+.

Sequence similarities

Belongs to the terpene synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    952
  • Mass (Da)
    106,762
  • Last updated
    2013-09-18 v1
  • Checksum
    E5E8C6D904C77A05
MPGKIENGTPKDLKTGNDFVSAAKSLLDRAFKSHHSYYGLCSTSCQVYDTAWVAMIPKTRDNVKQWLFPECFHYLLKTQAADGSWGSLPTTQTAGILDTASAVLALLCHAQEPLQILDVSPDEMGLRIEHGVTSLKRQLAVWNDVEDTNHIGVEFIIPALLSMLEKELDVPSFEFPCRSILERMHGEKLGHFDLEQVYGKPSSLLHSLEAFLGKLDFDRLSHHLYHGSMMASPSSTAAYLIGATKWDDEAEDYLRHVMRNGAGHGNGGISGTFPTTHFECSWIIATLLKGGFTLKQIDGDGLRGLSTILLEALRDENGVIGFAPRTADVDDTAKALLALSLVNQPVSPDIMIKVFEGKDHFTTFGSERDPSLTSNLHVLLSLLKQSNLSQYHPQILKTTLFTCRWWWGSDHCVKDKWNLSHLYPTMLLVEAFTEVLHLIDGGELSSLFDESFKCKIGLSIFQAVLRIILTQDNDGSWRGYREQTCYAILALVQARHVCFFTHMVDRLQSCVDRGFSWLKSCSFHSQDLTWTSKTAYEVGFVAEAYKLAALQSASLEVPAATIGHSVTSAVPSSDLEKYMRLVRKTALFSPLDEWGLMASIIESSFFVPLLQAQRVEIYPRDNIKVDEDKYLSIIPFTWVGCNNRSRTFASNRWLYDMMYLSLLGYQTDEYMEAVAGPVFGDVSLLHQTIDKVIDNTMGNLARANGTVHSGNGHQHESPNIGQVEDTLTRFTNSVLNHKDVLNSSSSDQDTLRREFRTFMHAHITQIEDNSRFSKQASSDAFSSPEQSYFQWVNSTGGSHVACAYSFAFSNCLMSANLLQGKDAFPSGTQKYLISSVMRHATNMCRMYNDFGSIARDNAERNVNSIHFPEFTLCNGTSQNLDERKERLLKIATYEQGYLDRALEALERQSRDDAGDRAGSKDMRKLKIVKLFCDVTDLYDQLYVIKDLSSSMK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HF679027
EMBL· GenBank· DDBJ
CCT69398.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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