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Protein

(+)-epi-alpha-bisabolol synthase

Gene
N/A
Organism
Phyla dulcis (Aztec sweet herb) (Lippia dulcis)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Sesquiterpene synthase involved in the biosynthesis of (+)-epi-alpha-bisabolol, a precursor of the natural sweetner hernandulcin.1 Publication

Catalytic activityi

(2E,6E)-farnesyl diphosphate + H2O = (+)-epi-alpha-bisabolol + diphosphate.1 Publication

Cofactori

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

Kineticsi

Kcat is 0.04 sec (-1) for (2E,6E)-farnesyl diphosphate.

  1. KM=4.8 µM for (2E,6E)-farnesyl diphosphate1 Publication

    Pathway:iterpenoid biosynthesis

    This protein is involved in the pathway terpenoid biosynthesis, which is part of Secondary metabolite biosynthesis.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi297 – 2971Magnesium 1By similarity
    Metal bindingi297 – 2971Magnesium 2By similarity
    Metal bindingi301 – 3011Magnesium 1By similarity
    Metal bindingi301 – 3011Magnesium 2By similarity
    Metal bindingi441 – 4411Magnesium 3By similarity
    Metal bindingi445 – 4451Magnesium 3By similarity
    Metal bindingi449 – 4491Magnesium 3By similarity

    GO - Molecular functioni

    • magnesium ion binding Source: InterPro
    • sesquiterpene synthase activity Source: UniProtKB

    GO - Biological processi

    • (+)-epi-alpha-bisabolol biosynthetic process Source: UniProtKB
    • farnesyl diphosphate catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00213.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    (+)-epi-alpha-bisabolol synthase (EC:4.2.3.138)
    Alternative name(s):
    Terpene synthase 8
    Short name:
    LdTPS8
    OrganismiPhyla dulcis (Aztec sweet herb) (Lippia dulcis)
    Taxonomic identifieri542674 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsLamialesVerbenaceaeLantaneaePhyla

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 546546(+)-epi-alpha-bisabolol synthasePRO_0000421955Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliJ7LH11.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi297 – 3015DDXXD motif

    Domaini

    The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg2+.By similarity

    Sequence similaritiesi

    Belongs to the terpene synthase family.Curated

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    1.50.30.10. 1 hit.
    InterProiIPR008949. Isoprenoid_synthase_dom.
    IPR001906. Terpene_synth_N.
    IPR005630. Terpene_synthase_metal-bd.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PfamiPF01397. Terpene_synth. 1 hit.
    PF03936. Terpene_synth_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 1 hit.
    SSF48576. SSF48576. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    J7LH11-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNSTSRRSAN YKPTIWNNEY LQSLNSIYGE KRFLEQAEKL KDEVRMLLEK
    60 70 80 90 100
    TSDPLDHIEL VDVLQRLAIS YHFTEYIDRN LKNIYDILID GRRWNHADNL
    110 120 130 140 150
    HATTLSFRLL RQHGYQVSPE VFRNFMDETG NFKKNLCDDI KGLLSLYEAS
    160 170 180 190 200
    YLLTEGETIM DSAQAFATHH LKQKLEENMN KNLGDEIAHA LELPLHWRVP
    210 220 230 240 250
    KLDVRWSIDA YERRQDMNPL LLELAKLDFN IAQSMYQDEL KELSRWYSKT
    260 270 280 290 300
    HLPEKLAFAR DRLVESYLWG LGLASEPHHK YCRMMVAQST TLISIIDDIY
    310 320 330 340 350
    DVYGTLDELQ LFTHAVDRWD IKYLEQLPEY MQICFLALFN TVNERSYDFL
    360 370 380 390 400
    LDKGFNVIPH SSYRWAELCK TYLIEANWYH SGYKPSLNEY LNQGLISVAG
    410 420 430 440 450
    PHALSHTYLC MTDSLKEKHI LDLRTNPPVI KWVSILVRLA DDLGTSTDEL
    460 470 480 490 500
    KRGDNPKSIQ CHMHDTGCNE EETRAYIKNL IGSTWKKINK DVLMNFEYSM
    510 520 530 540
    DFRTAAMNGA RVSQFMYQYD DDGHGVPEGK SKERVCSLIV EPIPLP
    Length:546
    Mass (Da):63,782
    Last modified:October 31, 2012 - v1
    Checksum:iDE64E5D3475494B5
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    JQ731636 mRNA. Translation: AFR23372.1.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    The taste of sweet - Issue 148 of May 2013

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    JQ731636 mRNA. Translation: AFR23372.1.

    3D structure databases

    ProteinModelPortaliJ7LH11.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00213.

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    1.50.30.10. 1 hit.
    InterProiIPR008949. Isoprenoid_synthase_dom.
    IPR001906. Terpene_synth_N.
    IPR005630. Terpene_synthase_metal-bd.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PfamiPF01397. Terpene_synth. 1 hit.
    PF03936. Terpene_synth_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 1 hit.
    SSF48576. SSF48576. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Molecular cloning and characterization of (+)-epi-alpha-bisabolol synthase, catalyzing the first step in the biosynthesis of the natural sweetener, hernandulcin, in Lippia dulcis."
      Attia M., Kim S.U., Ro D.K.
      Arch. Biochem. Biophys. 527:37-44(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiTPS8_PHYDL
    AccessioniPrimary (citable) accession number: J7LH11
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2013
    Last sequence update: October 31, 2012
    Last modified: April 1, 2015
    This is version 13 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.