ID   TPSD1_PSEMZ             Reviewed;          66 AA.
AC   P85964;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Alpha-bisabolene synthase {ECO:0000250|UniProtKB:O81086};
DE            EC=4.2.3.38;
DE   AltName: Full=(E)-alpha-bisabolene synthase {ECO:0000250|UniProtKB:O81086};
DE   Flags: Fragments;
OS   Pseudotsuga menziesii (Douglas-fir) (Abies menziesii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC   Pseudotsuga.
OX   NCBI_TaxID=3357;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004;
RA   Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.;
RT   "A proteomics approach to identify proteins differentially expressed in
RT   Douglas-fir seedlings infected by Phellinus sulphurascens.";
RL   J. Proteomics 71:425-438(2008).
CC   -!- FUNCTION: Involved in defensive oleoresin formation in conifers in
CC       response to insect attack or other injury. Involved in sesquiterpene
CC       (C15) olefins biosynthesis (By similarity).
CC       {ECO:0000250|UniProtKB:O81086}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (E,R)-alpha-bisabolene +
CC         diphosphate; Xref=Rhea:RHEA:25436, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:49243, ChEBI:CHEBI:175763; EC=4.2.3.38;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:O64404};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000250|UniProtKB:O64404};
CC   -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC       {ECO:0000250|UniProtKB:O81086}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC       {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P85964; -.
DR   SMR; P85964; -.
DR   UniPathway; UPA00924; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052681; F:alpha-bisabolene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.600.10; -; 2.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lyase; Manganese; Metal-binding.
FT   CHAIN           <1..>66
FT                   /note="Alpha-bisabolene synthase"
FT                   /id="PRO_0000392515"
FT   NON_CONS        7..8
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_CONS        29..30
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         66
FT                   /evidence="ECO:0000303|PubMed:18602030"
SQ   SEQUENCE   66 AA;  8105 MW;  9C9C220F03080F99 CRC64;
     RQERLAKLFT EAVRRWDVSF TENLPDYMKE LVSFFRKGWE DYLLGYYEEA EWLAAEYVPS
     LDEYIK