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Entry version 93 (02 Jun 2021)
Sequence version 1 (01 Nov 1998)
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Protein

Alpha-bisabolene synthase

Gene

ag1

Organism
Abies grandis (Grand fir) (Pinus grandis)
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 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

Converts farnesyl diphosphate to alpha-bisabolene (PubMed:9618485, PubMed:9539701, PubMed:22153510).

Involved in defensive oleoresin formation in conifers in response to insect attack or other injury (PubMed:9618485, PubMed:9539701).

Involved in sesquiterpene (C15) olefins biosynthesis (PubMed:9618485, PubMed:9539701).

3 Publications

Miscellaneous

The conserved 25-Arg-Arg-26 motif may play a role in the isomerization step of the terpenoid cyclization reaction sequence.

<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

Protein has several cofactor binding sites:

<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

  1. KM=49.5 µM for (2E,6E)-farnesyl diphosphate1 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: oleoresin biosynthesis

    This protein is involved in the pathway oleoresin biosynthesis, which is part of Terpene metabolism.Curated
    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 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 bindingi566Magnesium 1Combined sources1 Publication1
    Metal bindingi566Magnesium 2Combined sources1 Publication1
    Metal bindingi570Magnesium 1Combined sources1 Publication1
    Metal bindingi570Magnesium 2Combined sources1 Publication1
    Metal bindingi713Magnesium 3Combined sources1 Publication1
    Metal bindingi717Magnesium 3Combined sources1 Publication1
    Metal bindingi721Magnesium 3Combined sources1 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
    4.2.3.38, 2

    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:
    Alpha-bisabolene synthase (EC:4.2.3.382 Publications)
    Alternative name(s):
    (E)-alpha-bisabolene synthase
    AgfEabis
    <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:ag1
    <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>OrganismiAbies grandis (Grand fir) (Pinus grandis)
    <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 identifieri46611 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaPinopsidaPinidaePinalesPinaceaeAbies

    <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

    Cytoplasm

    <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>Mutagenesisi570D → A: Abolishes catalytic activity. 1 Publication1
    Mutagenesisi713D → A: Abolishes 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 polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001864461 – 817Alpha-bisabolene synthaseAdd BLAST817

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    O81086

    <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 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

    By wounding.1 Publication

    <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

    1817
    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
    O81086

    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>Motifi566 – 570DDXXD 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+.

    <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

    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
    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

    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.

    O81086-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAGVSAVSKV SSLVCDLSST SGLIRRTANP HPNVWGYDLV HSLKSPYIDS
    60 70 80 90 100
    SYRERAEVLV SEIKAMLNPA ITGDGESMIT PSAYDTAWVA RVPAIDGSAR
    110 120 130 140 150
    PQFPQTVDWI LKNQLKDGSW GIQSHFLLSD RLLATLSCVL VLLKWNVGDL
    160 170 180 190 200
    QVEQGIEFIK SNLELVKDET DQDSLVTDFE IIFPSLLREA QSLRLGLPYD
    210 220 230 240 250
    LPYIHLLQTK RQERLAKLSR EEIYAVPSPL LYSLEGIQDI VEWERIMEVQ
    260 270 280 290 300
    SQDGSFLSSP ASTACVFMHT GDAKCLEFLN SVMIKFGNFV PCLYPVDLLE
    310 320 330 340 350
    RLLIVDNIVR LGIYRHFEKE IKEALDYVYR HWNERGIGWG RLNPIADLET
    360 370 380 390 400
    TALGFRLLRL HRYNVSPAIF DNFKDANGKF ICSTGQFNKD VASMLNLYRA
    410 420 430 440 450
    SQLAFPGENI LDEAKSFATK YLREALEKSE TSSAWNNKQN LSQEIKYALK
    460 470 480 490 500
    TSWHASVPRV EAKRYCQVYR PDYARIAKCV YKLPYVNNEK FLELGKLDFN
    510 520 530 540 550
    IIQSIHQEEM KNVTSWFRDS GLPLFTFARE RPLEFYFLVA AGTYEPQYAK
    560 570 580 590 600
    CRFLFTKVAC LQTVLDDMYD TYGTLDELKL FTEAVRRWDL SFTENLPDYM
    610 620 630 640 650
    KLCYQIYYDI VHEVAWEAEK EQGRELVSFF RKGWEDYLLG YYEEAEWLAA
    660 670 680 690 700
    EYVPTLDEYI KNGITSIGQR ILLLSGVLIM DGQLLSQEAL EKVDYPGRRV
    710 720 730 740 750
    LTELNSLISR LADDTKTYKA EKARGELASS IECYMKDHPE CTEEEALDHI
    760 770 780 790 800
    YSILEPAVKE LTREFLKPDD VPFACKKMLF EETRVTMVIF KDGDGFGVSK
    810
    LEVKDHIKEC LIEPLPL
    Length:817
    Mass (Da):93,749
    Last modified:November 1, 1998 - 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:i95FB06DBC0DE1B4B
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti65A → V in AAC24191 (PubMed:9618485).Curated1
    Sequence conflicti65A → V in AAK83562 (PubMed:11404343).Curated1
    Sequence conflicti590L → V in AAK83562 (PubMed:11404343).Curated1
    Sequence conflicti655T → S in AAK83562 (PubMed:11404343).Curated1
    Sequence conflicti784R → G in AAK83562 (PubMed:11404343).Curated1

    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
    AF006195 mRNA Translation: AAC24192.1
    AF006194 mRNA Translation: AAC24191.1
    AF326515 Genomic DNA Translation: AAK83562.1

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:AAC24192

    <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
    AF006195 mRNA Translation: AAC24192.1
    AF006194 mRNA Translation: AAC24191.1
    AF326515 Genomic DNA Translation: AAK83562.1

    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
    3SAEX-ray1.96A1-817[»]
    3SDQX-ray2.14A1-817[»]
    3SDRX-ray1.86A1-817[»]
    3SDTX-ray1.89A1-817[»]
    3SDUX-ray1.89A1-817[»]
    3SDVX-ray2.20A1-817[»]
    SMRiO81086
    ModBaseiSearch...
    PDBe-KBiSearch...

    Proteomic databases

    PRIDEiO81086

    Genome annotation databases

    KEGGiag:AAC24192

    Enzyme and pathway databases

    UniPathwayiUPA00924
    BRENDAi4.2.3.38, 2

    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
    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
    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_ABIGR
    <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: O81086
    Secondary accession number(s): Q94FW2, Q9SAU6
    <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: April 12, 2005
    Last sequence update: November 1, 1998
    Last modified: June 2, 2021
    This is version 93 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

    Keywords - Technical termi

    3D-structure

    Documents

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