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Entry version 21 (02 Jun 2021)
Sequence version 1 (20 Jan 2016)
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Protein

Stellatatriene synthase

Gene

Stl-SS

Organism
Emericella variicolor (Aspergillus stellatus)
Status
Reviewed-Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: terpenoid biosynthesis

This protein is involved in the pathway terpenoid biosynthesis, which is part of Secondary metabolite biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway terpenoid biosynthesis and in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi92Magnesium 1By similarity1
Metal bindingi92Magnesium 2By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei92SubstrateBy similarity1
Metal bindingi96Magnesium 1By similarity1
Metal bindingi96Magnesium 2By similarity1
Binding sitei96SubstrateBy similarity1
Binding sitei434Isopentenyl diphosphateBy similarity1
Binding sitei437Isopentenyl diphosphateBy similarity1
Binding sitei466Isopentenyl diphosphateBy similarity1
Metal bindingi473Magnesium 3By similarity1
Metal bindingi473Magnesium 4By similarity1
Metal bindingi477Magnesium 3By similarity1
Metal bindingi477Magnesium 4By similarity1
Binding sitei482Dimethylallyl diphosphateBy similarity1
Binding sitei483Isopentenyl diphosphateBy similarity1
Binding sitei560Dimethylallyl diphosphateBy similarity1
Binding sitei561Dimethylallyl diphosphateBy similarity1
Binding sitei596Dimethylallyl diphosphateBy similarity1
Binding sitei603Dimethylallyl diphosphateBy similarity1
Binding sitei613Dimethylallyl diphosphateBy similarity1
Binding sitei623Dimethylallyl diphosphateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase, Multifunctional enzyme, Transferase
Biological processIsoprene biosynthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00213

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Stellatatriene synthase1 Publication
Short name:
SS1 Publication
Alternative name(s):
Stellatic acid biosynthetis gene clusters protein Stl-SS1 Publication
Including the following 2 domains:
Geranylgeranyl diphosphate synthase1 Publication (EC:2.5.1.-1 Publication)
Short name:
GGDP synthase1 Publication
Short name:
GGS1 Publication
stellata-2,6,19-trien synthase1 Publication (EC:4.2.3.1781 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Stl-SS1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEmericella variicolor (Aspergillus stellatus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1549217 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004525141 – 714Stellatatriene synthaseAdd BLAST714

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Hexamer.

By similarity

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
A0A0P0ZEM1

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 325stellata-2,6,19-trien synthaseBy similarityAdd BLAST325
Regioni179 – 182Substrate bindingBy similarity4
Regioni227 – 231Substrate bindingBy similarity5
Regioni316 – 317Substrate bindingBy similarity2
Regioni326 – 713Geranylgeranyl diphosphate synthaseBy similarityAdd BLAST388
Regioni632 – 633Substrate-bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi92 – 96DDXXD motif 11 Publication5
Motifi276 – 284NSE motif1 Publication9
Motifi473 – 477DDXXD motif 21 Publication5

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.1 Publication
The Mg2+-binding NSE motif in the terpene cyclase domain is not completely conserved, since the asparagine residue in the is substituted with histidine.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Keywords - Domaini

Repeat

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00685, Trans_IPPS_HT, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.600.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008949, Isoprenoid_synthase_dom_sf
IPR000092, Polyprenyl_synt
IPR033749, Polyprenyl_synt_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00348, polyprenyl_synt, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48576, SSF48576, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00723, POLYPRENYL_SYNTHASE_1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

A0A0P0ZEM1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEYKFSTVVD PGTYETHGLC EGYEVRYHKN AELEDIGCLR CQEHWRQSVG
60 70 80 90 100
PLGAFKGTLG NPFNLLSLVI PECLPDRLSI VGFANELAFI HDDVTDIVQY
110 120 130 140 150
GDAHNNDFKE AFNSMATTGS MENAASGKRA LQAYIAREMV RIDKERAIPT
160 170 180 190 200
IKAWAKFVDY GGRQETTRFT SEKEYTEYRI QDIGLWFWYG LLSFAMALDV
210 220 230 240 250
PEHEREMCHE VCRTAYVQIM LVHDLASWEK EKLNAAALGK DVITNIIFVL
260 270 280 290 300
MEEHGISEEE AKERCRETAK TLAADYLKIV EEYKARDDIS LDSRKYIESW
310 320 330 340 350
LYTISGNTVW SFICPRYNSS GSFSDHQLEL MKNGVPKDPA SGSTNGTSNG
360 370 380 390 400
TSNGTSHVAV NGNGHVTNDD LSANGIKTDG ELLSAITMEH LKNRNSFKLG
410 420 430 440 450
DHDQEVKSLH GHGQALDPRV LQAPYEYITA LPSKGLREQA IDALNVWFRV
460 470 480 490 500
PTAKLEIIKS ITTILHNASL MLDDVEDGSE LRRGKPATHN IFGLGQTINS
510 520 530 540 550
ANYQLVRALQ ELQKLGDARS LLVFTEELHN LYVGQSMDLY WTSNLVCPSM
560 570 580 590 600
HEYFQMIEHK TGGLFRLFGR LMAVHSTNPV QVDLTDFTNH LGRYFQTRDD
610 620 630 640 650
YQNLVSAEYT KQKGFCEDFE EGKFSLPMIH LMQTMPDNLV LRNVWTQRRV
660 670 680 690 700
NGTATHGQKQ TILNLMKEAG TLKFTQDSLG VLYSDVEKSV AELESKFGIE
710
NFQLRLIMEL LKTG
Length:714
Mass (Da):80,706
Last modified:January 20, 2016 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDA520A976523611F
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
LC073704 Genomic DNA Translation: BAT32889.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:BAT32889

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LC073704 Genomic DNA Translation: BAT32889.1

3D structure databases

SMRiA0A0P0ZEM1
ModBaseiSearch...

Genome annotation databases

KEGGiag:BAT32889

Enzyme and pathway databases

UniPathwayiUPA00213

Family and domain databases

CDDicd00685, Trans_IPPS_HT, 1 hit
Gene3Di1.10.600.10, 2 hits
InterProiView protein in InterPro
IPR008949, Isoprenoid_synthase_dom_sf
IPR000092, Polyprenyl_synt
IPR033749, Polyprenyl_synt_CS
PfamiView protein in Pfam
PF00348, polyprenyl_synt, 1 hit
SUPFAMiSSF48576, SSF48576, 2 hits
PROSITEiView protein in PROSITE
PS00723, POLYPRENYL_SYNTHASE_1, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSTLSS_EMEVA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A0A0P0ZEM1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 2, 2021
Last sequence update: January 20, 2016
Last modified: June 2, 2021
This is version 21 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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