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Entry version 14 (02 Jun 2021)
Sequence version 1 (16 Mar 2016)
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Protein

Geranylfarnesyl diphosphate synthase, chloroplastic

Gene

GFDPS

Organism
Leucosceptrum canum (Hairy white-wand) (Clerodendron leucosceptrum)
Status
Reviewed-Annotation score:

Annotation score:5 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

Involved in the biosynthesis of leucosceptrane sesterterpenoids natural products, which are playing defensive roles toward herbivorus insects (e.g. Spodoptera exigua) (PubMed:26941091).

Catalyzes the condensation of isopentenyl pyrophosphate (IDP) with the allylic pyrophosphates to yield geranylfarnesyl diphosphate (GFDP), the C(25) prenyl diphosphate precursor to all sesterterpenoids (PubMed:26941091).

Geranylgeranyl diphosphate (GGPP) is the preferred substrate, however dimethylallyl diphosphate (DMADP), farnesyl diphosphate (FDP) and geranyl diphosphate (GDP) can also be used as allylic substrate (PubMed:26941091).

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 '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 2 Mg2+ ions per subunit.By similarity

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 16.9x10(-6) sec(-1) with dimethylallyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 8.2x10(-6) sec(-1) with isopentenyl diphosphate as substrate (in the presence of geranylgeranyl diphosphate) (PubMed:26941091). kcat is 6.16x10(-6) sec(-1) with geranyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 7.19x10(-6) sec(-1) with farnesyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 5.17x10(-6) sec(-1) with geranylgeranyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091).1 Publication
  1. KM=34.89 µM for dimethylallyl diphosphate (in the presence of isopentenyl diphosphate)1 Publication
  2. KM=3.04 µM for isopentenyl diphosphate (in the presence of geranylgeranyl diphosphate)1 Publication
  3. KM=6.28 µM for geranyl diphosphate (in the presence of isopentenyl diphosphate)1 Publication
  4. KM=4.10 µM for farnesyl diphosphate (in the presence of isopentenyl diphosphate)1 Publication
  5. KM=1.65 µM for geranylgeranyl diphosphate (in the presence of isopentenyl diphosphate)1 Publication

    <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.

    Pathwayi: Isoprenoid biosynthesis

    This protein is involved in Isoprenoid biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in Isoprenoid biosynthesis.

    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 sitei72Isopentenyl diphosphateBy similarity1
    Binding sitei111Isopentenyl diphosphateBy similarity1
    Binding sitei143Isopentenyl diphosphateBy 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 bindingi150Magnesium 1By similarity1
    Metal bindingi150Magnesium 2By similarity1
    Metal bindingi156Magnesium 1By similarity1
    Metal bindingi156Magnesium 2By similarity1
    Binding sitei161Dimethylallyl diphosphateBy similarity1
    Binding sitei162Isopentenyl diphosphateBy similarity1
    Binding sitei249Dimethylallyl diphosphateBy similarity1
    Binding sitei250Dimethylallyl diphosphateBy similarity1
    Binding sitei287Dimethylallyl diphosphateBy similarity1
    Binding sitei294Dimethylallyl diphosphateBy similarity1
    Binding sitei304Dimethylallyl diphosphateBy similarity1
    Binding sitei314Dimethylallyl 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 - Molecular functioni

    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 functionTransferase
    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:
    Geranylfarnesyl diphosphate synthase, chloroplastic1 Publication (EC:2.5.1.811 Publication)
    Short name:
    LcGFDPS1 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:GFDPS1 Publication
    Synonyms:IDS31 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>OrganismiLeucosceptrum canum (Hairy white-wand) (Clerodendron leucosceptrum)
    <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 identifieri694369 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaeasteridslamiidsLamialesLamiaceaeLamioideaePogostemoneaeLeucosceptrum

    <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 – 51ChloroplastSequence analysisAdd BLAST51
    <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_000045269152 – 364Geranylfarnesyl diphosphate synthase, chloroplasticAdd BLAST313

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Strongly expressed in glandular trichomes, and, at low levels, in leaves, stems and flowers.1 Publication

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Induced by jasmonic acid, thus triggering sesterterpenoids accumulation and reducing feeding and growth of the herbivorus insect Spodoptera exigua (PubMed:26941091). Accumulates transiently after salicylic acid treatment (PubMed:26941091).1 Publication

    <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

    Monomer.

    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
    A0A0U3BRC5

    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

    <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 FPP/GGPP synthase family.Curated

    Keywords - Domaini

    Transit peptide

    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, 1 hit

    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, 1 hit

    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.

    <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.

    A0A0U3BRC5-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSHCTIFLYK YFPGKPRYQH CSFLHPLNHK LKSLFLPITG SRFLSNSTFS
    60 70 80 90 100
    VSDSAHSHQA KPHVRNAQFD FKAYMLEKIT AVNQALDAAL PVREPVKIHE
    110 120 130 140 150
    AMRYSLLLGG KRICPIVCLA ACHLVGGDES TAMPSAAALE MIHAMSLMHD
    160 170 180 190 200
    DLPCMDNDDL RRGRPSNHVV FGEGATVLAG YALIARAFEH IATATQGVGP
    210 220 230 240 250
    GKILRVIGEL AQLIGAEGVV GGQVVDLRCG GEGQMAIGLE QLEYIHLHKT
    260 270 280 290 300
    AASVEASAVA GAVLGGASEE EIERLRKYSR SAGLLFQVVD DILDVTKSSE
    310 320 330 340 350
    ELGKTAGKDL AAGKTTYPKL LGMEKSREMA EKLKREAQEQ LLGFDPIKAA
    360
    PLIALVDFIA YRDK
    Length:364
    Mass (Da):39,476
    Last modified:March 16, 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:iE4929C92D224C5C4
    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
    KT312959 mRNA Translation: ALT16903.1

    <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
    KT312959 mRNA Translation: ALT16903.1

    3D structure databases

    SMRiA0A0U3BRC5
    ModBaseiSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00213

    Family and domain databases

    CDDicd00685, Trans_IPPS_HT, 1 hit
    Gene3Di1.10.600.10, 1 hit
    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, 1 hit
    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 nameiGFDPS_LEUCN
    <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: A0A0U3BRC5
    <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: March 16, 2016
    Last modified: June 2, 2021
    This is version 14 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
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