Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - Q675L4 (TPSD1_PICAB)

Entry version 74 (25 May 2022)
Sequence version 1 (11 Oct 2004)
Previous versions | rss
Add a publicationFeedback
Protein

Bifunctional levopimaradiene synthase, chloroplastic

Gene

TPS-LAS

Organism
Picea abies (Norway spruce) (Picea excelsa)
Status
Reviewed-Annotation score:

Annotation score:4 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 transcript 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

Involved in defensive oleoresin formation in conifers in response to insect attack or other injury (By similarity).

Involved in diterpene (C20) olefins biosynthesis. Bifunctional enzyme that catalyzes two sequential cyclizations of geranylgeranyl diphosphate (GGPP) to levopimaradiene. Levopimaradiene is the major products of the enzyme followed by abietadiene, neoabietadiene and palustradiene.

By similarity1 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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarityNote: Binds 3 Mg2+ ions per subunit.By similarity

<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: oleoresin biosynthesis

This protein is involved in the pathway oleoresin biosynthesis, which is part of Terpene metabolism.
View all proteins of this organism that are known to be involved in the pathway oleoresin biosynthesis and in Terpene metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei259SubstrateBy similarity1
<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 bindingi392Magnesium 4By similarity1
Metal bindingi394Magnesium 4By similarity1
Binding sitei479SubstrateBy similarity1
Metal bindingi611Magnesium 1By similarity1
Metal bindingi611Magnesium 2By similarity1
Metal bindingi615Magnesium 1By similarity1
Metal bindingi615Magnesium 2By similarity1
Metal bindingi755Magnesium 3By similarity1
Metal bindingi759Magnesium 3By similarity1
Metal bindingi763Magnesium 3By 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 - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionIsomerase, Lyase, Multifunctional enzyme
Biological processPlant defense
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		4.2.3.18, 4815
4.2.3.32, 4815
5.5.1.12, 4815

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

More...UniPathwayi		UPA00924

<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:
Bifunctional levopimaradiene synthase, chloroplastic
Alternative name(s):
Diterpene synthase
PaTPS-LAS
Including the following 2 domains:
Levopimaradiene synthase (EC:4.2.3.32)
Copalyl diphosphate synthase (EC:5.5.1.12)
<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:TPS-LAS
<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>OrganismiPicea abies (Norway spruce) (Picea excelsa)
<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 identifieri3329 [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 lineageiEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Pinopsida › Pinidae › Conifers I › Pinales › Pinaceae › Picea

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Chloroplast, Plastid

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 70ChloroplastSequence analysisAdd BLAST70
<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_000034895271 – 859Bifunctional levopimaradiene synthase, chloroplasticAdd BLAST789

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		Q675L4

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

More...SMRi		Q675L4

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

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>Motifi392 – 395DXDD motifCurated4
Motifi611 – 615DDXXD motifCurated5

<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 Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity in the class II active site relevant for the cyclization of GGPP. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity in the class I active site, presumably through binding to Mg2+.Curated

<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

Belongs to the terpene synthase family. Tpsd subfamily.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Conserved Domains Database

More...CDDi		cd00684, Terpene_cyclase_plant_C1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.600.10, 1 hit
1.50.10.130, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR008949, Isoprenoid_synthase_dom_sf
IPR034741, Terpene_cyclase-like_1_C
IPR044814, Terpene_cyclase_plant_C1
IPR001906, Terpene_synth_N
IPR036965, Terpene_synth_N_sf
IPR005630, Terpene_synthase_metal-bd
IPR008930, Terpenoid_cyclase/PrenylTrfase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01397, Terpene_synth, 1 hit
PF03936, Terpene_synth_C, 1 hit

Structure-Function Linkage Database

More...SFLDi		SFLDG01019, Terpene_Cyclase_Like_1_C_Termi, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48239, SSF48239, 2 hits
SSF48576, SSF48576, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q675L4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALLSSSLSS QIPTGAHHLT LNAYANTQCI PHFFSTLNAG TSAGKRSSLY 
        60         70         80         90        100
LRWGKGSNKI IACVGEDSLS APTLVKREFP PGFWKDHVID SLTSSHKVAA 
       110        120        130        140        150
SDEKRIETLI SEIKNMFRSM GYGDTNPSAY DTAWVARIPA VDGSEQPEFP 
       160        170        180        190        200
ETLEWILQNQ LKDGSWGEGF YFLAYDRILA TLACIITLTL WRTGEIQVQK 
       210        220        230        240        250
GIEFFKTQAG KIEDEADSHR PSGFEIVFPA MLKEAKVLGL DLPYELPFIK 
       260        270        280        290        300
QIIEKREAKL ERLPTNILYA LPTTLLYSLE GLQEIVDWQK IIKLQSKDGS 
       310        320        330        340        350
FLSSPASTAA VFMRTGNKKC LEFLNFVLKK FGNHVPCHYP LDLFERLWAV 
       360        370        380        390        400
DTIERLGIDR HFKEEIKDAL DYVYSHWDER GIGWARENPV PDIDDTAMGL 
       410        420        430        440        450
RILRLHGYNV SSDVLKTFRD ENGEFFCFLG QTQRGVTDML NVNRCSHVAF 
       460        470        480        490        500
PGETIMEEAK TCTERYLRNA LEDVGAFDKW ALKKNIRGEV EYALKYPWHR 
       510        520        530        540        550
SMPRLEARSY IEHYGPNDVW LGKTMYMMPY ISNEKYLELA KLDFNHVQSL 
       560        570        580        590        600
HQKELRDLRR WWTSSGFTEL KFTRERVTEI YFSPASFMFE PEFATCRAVY 
       610        620        630        640        650
TKTSNFTVIL DDLYDAHGTL DDLKLFSDSV KKWDLSLVDR MPQDMKICFM 
       660        670        680        690        700
GFYNTFNEIA EEGRKRQGRD VLGYIRNVWE IQLEAYTKEA EWSAARYVPS 
       710        720        730        740        750
FDEYIDNASV SIALGTVVLI SALFTGEILT DDVLSKIGRG SRFLQLMGLT 
       760        770        780        790        800
GRLVNDTKTY EAERGQGEVA SAVQCYMKDH PEISEEEALK HVYTVMENAL 
       810        820        830        840        850
DELNREFVNN REVPDSCRRL VFETARIMQL FYMDGDGLTL SHETEIKEHV 

KNCLFQPVA
Length:859
Mass (Da):98,458
Last modified:October 11, 2004 - 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:iBD98408794AC8CAB
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AY473621 mRNA Translation: AAS47691.1

<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
AY473621 mRNA Translation: AAS47691.1

3D structure databases

AlphaFoldDBiQ675L4
SMRiQ675L4
ModBaseiSearch...

Enzyme and pathway databases

UniPathwayiUPA00924
BRENDAi4.2.3.18, 4815
4.2.3.32, 4815
5.5.1.12, 4815

Family and domain databases

CDDicd00684, Terpene_cyclase_plant_C1, 1 hit
Gene3Di1.10.600.10, 1 hit
1.50.10.130, 1 hit
InterProiView protein in InterPro
IPR008949, Isoprenoid_synthase_dom_sf
IPR034741, Terpene_cyclase-like_1_C
IPR044814, Terpene_cyclase_plant_C1
IPR001906, Terpene_synth_N
IPR036965, Terpene_synth_N_sf
IPR005630, Terpene_synthase_metal-bd
IPR008930, Terpenoid_cyclase/PrenylTrfase
PfamiView protein in Pfam
PF01397, Terpene_synth, 1 hit
PF03936, Terpene_synth_C, 1 hit
SFLDiSFLDG01019, Terpene_Cyclase_Like_1_C_Termi, 1 hit
SUPFAMiSSF48239, SSF48239, 2 hits
SSF48576, SSF48576, 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 nameiTPSD1_PICAB
<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: Q675L4
<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: September 2, 2008
Last sequence update: October 11, 2004
Last modified: May 25, 2022
This is version 74 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 programPlant 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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.

Do not show this banner again