A0A0P0ZEM1 · STLSS_EMEVA

Function

function

Multifunctional diterpene synthase; part of the gene cluster that mediates the biosynthesis of the sesterterpene stellatic acid (PubMed:26351860).
The first step in the pathway is performed by the stellatatriene synthase that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and then converting GGDP into stellata-2,6,19-triene (PubMed:26351860).
The cytochrome P450 monooxygenase Stl-P450 then catalyzes three successive oxidation reactions on the C-20 methyl group to generate the carboxylic acid of stellatic acid (PubMed:26351860).

Catalytic activity

Pathway

Secondary metabolite biosynthesis; terpenoid biosynthesis.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site92Mg2+ 1 (UniProtKB | ChEBI)
Binding site92Mg2+ 2 (UniProtKB | ChEBI)
Binding site92substrate
Binding site96Mg2+ 1 (UniProtKB | ChEBI)
Binding site96Mg2+ 2 (UniProtKB | ChEBI)
Binding site96substrate
Binding site179-182substrate
Binding site227-231substrate
Binding site316-317substrate
Binding site434isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site437isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site466isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site473Mg2+ 3 (UniProtKB | ChEBI)
Binding site473Mg2+ 4 (UniProtKB | ChEBI)
Binding site477Mg2+ 3 (UniProtKB | ChEBI)
Binding site477Mg2+ 4 (UniProtKB | ChEBI)
Binding site482dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site483isopentenyl diphosphate (UniProtKB | ChEBI)
Binding site560dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site561dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site596dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site603dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site613dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site623dimethylallyl diphosphate (UniProtKB | ChEBI)
Binding site632-633substrate

GO annotations

AspectTerm
Molecular Functionlyase activity
Molecular Functionmetal ion binding
Molecular Functionprenyltransferase activity
Biological Processalcohol 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
    Stellatatriene synthase
  • Short names
    SS
  • Alternative names
    • Stellatic acid biosynthetis gene clusters protein Stl-SS

Including 2 domains:

  • Recommended name
    Geranylgeranyl diphosphate synthase
  • EC number
  • Short names
    GGDP synthase
    ; GGS
  • Recommended name
    stellata-2,6,19-trien synthase
  • EC number

Gene names

    • Name
      Stl-SS

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 12069 / CBS 136.55 / IMI 60316 / NBRC 32302
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes

Accessions

  • Primary accession
    A0A0P0ZEM1

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004525141-714Stellatatriene synthase

Interaction

Subunit

Hexamer.

Family & Domains

Features

Showing features for region, motif, compositional bias.

TypeIDPosition(s)Description
Region1-325stellata-2,6,19-trien synthase
Motif92-96DDXXD motif 1
Motif276-284NSE motif
Region326-713Geranylgeranyl diphosphate synthase
Region332-356Disordered
Compositional bias338-356Polar residues
Motif473-477DDXXD motif 2

Domain

The characteristic DDXXD motif for binding a trinuclear Mg2+ cluster is conserved in both the N-terminal terpene cyclase and C-terminal prenyl transferase domains.
The Mg2+-binding NSE motif in the terpene cyclase domain is not completely conserved, since the asparagine residue in the is substituted with histidine.

Sequence similarities

In the N-terminal section; belongs to the terpene synthase family.
In the C-terminal section; belongs to the FPP/GGPP synthase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    714
  • Mass (Da)
    80,706
  • Last updated
    2016-01-20 v1
  • Checksum
    DA520A976523611F
MEYKFSTVVDPGTYETHGLCEGYEVRYHKNAELEDIGCLRCQEHWRQSVGPLGAFKGTLGNPFNLLSLVIPECLPDRLSIVGFANELAFIHDDVTDIVQYGDAHNNDFKEAFNSMATTGSMENAASGKRALQAYIAREMVRIDKERAIPTIKAWAKFVDYGGRQETTRFTSEKEYTEYRIQDIGLWFWYGLLSFAMALDVPEHEREMCHEVCRTAYVQIMLVHDLASWEKEKLNAAALGKDVITNIIFVLMEEHGISEEEAKERCRETAKTLAADYLKIVEEYKARDDISLDSRKYIESWLYTISGNTVWSFICPRYNSSGSFSDHQLELMKNGVPKDPASGSTNGTSNGTSNGTSHVAVNGNGHVTNDDLSANGIKTDGELLSAITMEHLKNRNSFKLGDHDQEVKSLHGHGQALDPRVLQAPYEYITALPSKGLREQAIDALNVWFRVPTAKLEIIKSITTILHNASLMLDDVEDGSELRRGKPATHNIFGLGQTINSANYQLVRALQELQKLGDARSLLVFTEELHNLYVGQSMDLYWTSNLVCPSMHEYFQMIEHKTGGLFRLFGRLMAVHSTNPVQVDLTDFTNHLGRYFQTRDDYQNLVSAEYTKQKGFCEDFEEGKFSLPMIHLMQTMPDNLVLRNVWTQRRVNGTATHGQKQTILNLMKEAGTLKFTQDSLGVLYSDVEKSVAELESKFGIENFQLRLIMELLKTG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias338-356Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LC073704
EMBL· GenBank· DDBJ
BAT32889.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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