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Entry version 21 (02 Jun 2021)
Sequence version 2 (10 May 2017)
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Protein

(R)-limonene synthase 1, chloroplastic

Gene
N/A
Organism
Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis)
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

Catalyzes the conversion of geranyl diphosphate to (+)-(4R)-limonene (PubMed:28272875, PubMed:28272876).

Produces exclusively the (+)-enantiomer (PubMed:28272875).

Can use neryl diphosphate as substrate (PubMed:28272876).

Has no activity with farnesyl diphosphate (PubMed:28272875).

2 Publications

<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+1 Publication, Mn2+1 PublicationNote: Binds 3 Mg2+ or Mn2+ ions per subunit (PubMed:28272876). The best cofactor is Mn2+ (PubMed:28272875). No effect with monovalent cations (PubMed:28272875).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by 2-fluorogeranyl diphosphate (FGPP) and 2-fluoroneryl diphosphate (FNPP).1 Publication

<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 0.186 sec(-1) for geranyl diphosphate in presence of manganese. kcat is 0.118 sec(-1) for geranyl diphosphate in presence of magnesium. kcat is 0.43 sec(-1) for neryl diphosphate.2 Publications
  1. KM=13.1 µM for geranyl diphosphate in presence of manganese1 Publication
  2. KM=35 µM for geranyl diphosphate in presence of magnesium1 Publication
  3. KM=9 µM for neryl diphosphate1 Publication

    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 bindingi343Manganese 11 Publication1
    Metal bindingi343Manganese 21 Publication1
    <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 sitei343Substrate1 Publication1
    Metal bindingi347Manganese 11 Publication1
    Metal bindingi347Manganese 21 Publication1
    Binding sitei347Substrate1 Publication1
    Binding sitei485Substrate1 Publication1
    Metal bindingi488Manganese 31 Publication1
    Binding sitei488Substrate1 Publication1
    Binding sitei504Substrate1 Publication1

    <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

    <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
    LigandMagnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.2.3.20, 1426

    <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:
    (R)-limonene synthase 1, chloroplastic1 Publication (EC:4.2.3.202 Publications)
    Alternative name(s):
    (+)-limonene synthase 1
    <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>OrganismiCitrus sinensis (Sweet orange) (Citrus aurantium var. sinensis)Imported
    <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 identifieri2711 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsSapindalesRutaceaeAurantioideaeCitrus

    <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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi565Y → F: 50-fold decreased catalytic activity. 1 Publication1

    <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 – 52Chloroplast1 PublicationAdd BLAST52
    <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_000044024453 – 607(R)-limonene synthase 1, chloroplasticAdd BLAST555

    <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

    Secondary structure

    1607
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    A0A1C9J6A7

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    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>Motifi343 – 347DDXXD 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-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, 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.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG502QUH3, Eukaryota

    Family and domain databases

    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
    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, 1 hit
    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.

    A0A1C9J6A7-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSSCINPSTL ATSVNGFKCL PLATNRAAIR IMAKNKPVQC LVSTKYDNLT
    60 70 80 90 100
    VDRRSANYQP SIWDHDFLQS LNSNYTDETY KRRAEELKGK VKTAIKDVTE
    110 120 130 140 150
    PLDQLELIDN LQRLGLAYHF EPEIRNILRN IHNHNKDYNW RKENLYATSL
    160 170 180 190 200
    EFRLLRQHGY PVSQEVFSGF KDDKVGFICD DFKGILSLHE ASYYSLEGES
    210 220 230 240 250
    IMEEAWQFTS KHLKEMMITS NSKEEDVFVA EQAKRALELP LHWKAPMLEA
    260 270 280 290 300
    RWFIHVYEKR EDKNHLLLEL AKLEFNTLQA IYQEELKDIS GWWKDTGLGE
    310 320 330 340 350
    KLSFARNRLV ASFLWSMGIA FEPQFAYCRR VLTISIALIT VIDDIYDVYG
    360 370 380 390 400
    TLDELEIFTD AVARWDINYA LKHLPGYMKM CFLALYNFVN EFAYYVLKQQ
    410 420 430 440 450
    DFDMLLSIKH AWLGLIQAYL VEAKWYHSKY TPKLEEYLEN GLVSITGPLI
    460 470 480 490 500
    ITISYLSGTN PIIKKELEFL ESNPDIVHWS SKIFRLQDDL GTSSDEIQRG
    510 520 530 540 550
    DVPKSIQCYM HETGASEEVA REHIKDMMRQ MWKKVNAYTA DKDSPLTRTT
    560 570 580 590 600
    AEFLLNLVRM SHFMYLHGDG HGVQNQETID VGFTLLFQPI PLEDKDMAFT

    ASPGTKG
    Length:607
    Mass (Da):70,354
    Last modified:May 10, 2017 - v2
    <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:iF1A481732DDE2B95
    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
    KU746814 mRNA Translation: AOP12358.2

    <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
    KU746814 mRNA Translation: AOP12358.2

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5UV0X-ray2.30A1-607[»]
    5UV1X-ray2.40A1-607[»]
    5UV2X-ray2.20A1-607[»]
    6ONMX-ray2.70A1-607[»]
    SMRiA0A1C9J6A7
    ModBaseiSearch...
    PDBe-KBiSearch...

    Phylogenomic databases

    eggNOGiENOG502QUH3, Eukaryota

    Enzyme and pathway databases

    BRENDAi4.2.3.20, 1426

    Family and domain databases

    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
    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, 1 hit
    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 nameiRLC1_CITSI
    <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: A0A1C9J6A7
    <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 7, 2017
    Last sequence update: May 10, 2017
    Last modified: June 2, 2021
    This is version 21 of the entry and version 2 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

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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