A0A1U8QLG8 · PBCB_EMENI

Function

function

Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the diterpene ent-pimara-814,15-diene (PD) (PubMed:22506079, PubMed:27098256).
Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:22506079, PubMed:27098256).
The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes (PubMed:22506079, PubMed:27098256).
Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara-814,15-diene (PubMed:22506079, PubMed:27098256).
The putative roles of the remaining cluster enzymes in ent-pimara-814,15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-814,15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 3 Mg2+ ions per subunit.

Pathway

Secondary metabolite biosynthesis; terpenoid biosynthesis.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site120isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site123isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site152isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site159Mg2+ 1 (UniProtKB | ChEBI)
Binding site159Mg2+ 2 (UniProtKB | ChEBI)
Binding site163Mg2+ 1 (UniProtKB | ChEBI)
Binding site163Mg2+ 2 (UniProtKB | ChEBI)
Binding site168dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site169isopentenyl diphosphate (UniProtKB | ChEBI)
Site191Important for determining product chain length
Binding site247dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site248dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site281dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site284Mg2+ 3 (UniProtKB | ChEBI)
Binding site288dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site298dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site308dimethylallyl diphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functiondimethylallyltranstransferase activity
Molecular Functionfarnesyltranstransferase activity
Molecular Functiongeranyltranstransferase activity
Molecular Functionmetal ion binding
Molecular Functionprenyltransferase activity
Biological Processalcohol biosynthetic process
Biological Processisoprenoid biosynthetic process
Biological Processketone biosynthetic process
Biological Processmycotoxin biosynthetic process
Biological Processterpenoid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Geranylgeranyl pyrophosphate synthase AN1592
  • EC number
  • Short names
    GGPP synthase
    ; GGPPSase
  • 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

    • ORF names
      AN1592, ANIA_01592

Organism names

Accessions

  • Primary accession
    A0A1U8QLG8
  • Secondary accessions
    • C8VN85
    • Q5BCY8

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004508401-397Geranylgeranyl pyrophosphate synthase AN1592

Expression

Induction

Expression is positively regulated by the cluster-specific transcription factor pbcR.

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-67Disordered
Compositional bias17-39Basic and acidic residues
Compositional bias47-67Polar residues

Sequence similarities

Belongs to the FPP/GGPP synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    397
  • Mass (Da)
    45,185
  • Last updated
    2017-05-10 v1
  • Checksum
    46E5E26D2E851FA6
MSPPLDSALEPLSEYKETAFPRTEKDPSQYKEHDLVTPEKEIQTGYFSPRGSHSSHGSHDSSASSNISLDDARMSDVNNSPNVFHDDPDTIDEKLSMYWKAANETVIREPYDYIAGIPGKEIRRKLLEAFNHWYKVDEQSCQAIATTVGMAHNASLLIDDIQDSSKLRRGVPCAHEVFGIAQTINSANYVYFLAQNQLFRLRSWPQAISVFNEEMVNLHRGQGMELFWRDNLLPPSMDDYLQMIANKTGGLFRMIVRLLQTSSRQVIDVEQLVDVLGLYFQILDDYKNIREEKMAAQKGFFEDLTEGKFSFPICHAIGEGAKNRTALLHMLRLKTDDMKIKQEAVCILDNAGSLDYTREVLYGLDRKARSLLREFKTPNPFMEALLDAMLSSLQACH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias17-39Basic and acidic residues
Compositional bias47-67Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AACD01000025
EMBL· GenBank· DDBJ
EAA64299.1
EMBL· GenBank· DDBJ
Genomic DNA
BN001307
EMBL· GenBank· DDBJ
CBF85177.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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