S0E627 · GA5_GIBF5

Function

function

Geranylgeranyl pyrophosphate 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 site109isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site112isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site141isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site148Mg2+ 1 (UniProtKB | ChEBI)
Binding site148Mg2+ 2 (UniProtKB | ChEBI)
Binding site152Mg2+ 1 (UniProtKB | ChEBI)
Binding site152Mg2+ 2 (UniProtKB | ChEBI)
Binding site157dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site158isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site235dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site236dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site275dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site278Mg2+ 3 (UniProtKB | ChEBI)
Binding site282dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site292dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site302dimethylallyl diphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functiondimethylallyltranstransferase activity
Molecular Functionfarnesyltranstransferase activity
Molecular Functiongeranyltranstransferase activity
Molecular Functionmetal ion binding
Biological Processalcohol biosynthetic process
Biological Processgibberellin biosynthetic process
Biological Processketone biosynthetic process
Biological Processmycotoxin biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Geranylgeranyl pyrophosphate synthase 2
  • EC number
  • Short names
    GGPP synthase 2
    ; GGPPSase 2
    ; GGS2
  • Alternative names
    • (2E,6E)-farnesyl diphosphate synthase
    • Dimethylallyltranstransferase
      (EC:2.5.1.1
      ) . EC:2.5.1.1 (UniProtKB | ENZYME | Rhea)
    • Farnesyl diphosphate synthase
    • Farnesyltranstransferase
      (EC:2.5.1.29
      ) . EC:2.5.1.29 (UniProtKB | ENZYME | Rhea)
    • Geranylgeranyl diphosphate synthase

Gene names

    • Name
      GGS2
    • ORF names
      FFUJ_14335

Organism names

Accessions

  • Primary accession
    S0E627

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004420451-393Geranylgeranyl pyrophosphate synthase 2

Expression

Induction

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

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    393
  • Mass (Da)
    43,836
  • Last updated
    2013-09-18 v1
  • Checksum
    93C2D17169F1065C
MAEQQISNLLSMFDASHASQKLEITVQMMDTYHYRETPPDSSSSEGGSLSRYDERRVSLPLSHNAASPDIVSQLCFSTAMSSELNHRWKSQRLKVADSPYNYILTLPSKGIRGAFIDSLNVWLEVPEDETSVIKEVIGMLHNSSLIIDDFQDNSPLRRGKPSTHTVFGPAQAINTATYVIVKAIEKIQDIVGHDALADVTGTITTIFQGQAMDLWWTANAIVPSIQEYLLMVNDKTGALFRLSLELLALNSEASISDSALESLSSAVSLLGQYFQIRDDYMNLIDNKYTDQKGFCEDLDEGKYSLTLIHALQTDSSDLLTNILSMRRVQGKLTAQQKMLVLEVMKTNGSLDWTSKLLGMLHTRVVAEIESLEVSTKRDNHALRALVERLKLET

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HF679027
EMBL· GenBank· DDBJ
CCT69172.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help