TPSBS_PSEMZ
ID TPSBS_PSEMZ Reviewed; 815 AA.
AC Q4QSN4;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=(E)-gamma-bisabolene synthase;
DE Short=PmeTPS3;
DE EC=4.2.3.59;
GN Name=TPS3;
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 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY
RP METHYL JASMONATE.
RX PubMed=15921711; DOI=10.1016/j.phytochem.2005.04.030;
RA Huber D.P., Philippe R.N., Godard K.A., Sturrock R.N., Bohlmann J.;
RT "Characterization of four terpene synthase cDNAs from methyl jasmonate-
RT induced Douglas-fir, Pseudotsuga menziesii.";
RL Phytochemistry 66:1427-1439(2005).
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. Produces mainly (E)-gamma-bisabolene when
CC used with farnesyl diphosphate as substrate. No activity with geranyl
CC diphosphate or geranylgeranyl diphosphate.
CC {ECO:0000269|PubMed:15921711}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (E)-gamma-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:28298, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49239, ChEBI:CHEBI:175763; EC=4.2.3.59;
CC Evidence={ECO:0000269|PubMed:15921711};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by methyl jasmonate.
CC {ECO:0000269|PubMed:15921711}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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 EMBL; AY906868; AAX07266.1; -; mRNA.
DR AlphaFoldDB; Q4QSN4; -.
DR SMR; Q4QSN4; -.
DR PRIDE; Q4QSN4; -.
DR KEGG; ag:AAX07266; -.
DR BioCyc; MetaCyc:MON-16024; -.
DR BRENDA; 4.2.3.59; 5214.
DR UniPathway; UPA00924; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..815
FT /note="(E)-gamma-bisabolene synthase"
FT /id="PRO_0000412238"
FT MOTIF 561..565
FT /note="DDXXD motif"
FT BINDING 561
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 561
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 565
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 709
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 717
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 815 AA; 93717 MW; A15F575A326C513E CRC64;
MAASTLPSGL STNDLIRRTA NPHPNVWGYD LLCSLKSPYS RDSSYKERAD TLINEIKAML
GAAFGDGKEM ITPSAYDTAW VARIPSIDGS SGSARPQFPQ TVDWILKNQL KDGSWGTESH
FLLSEPLLAT ISCVLALFKW QVGDLQVERG IEFLKSSLEK IKNESDQDSL VTDFEIIFPS
MLREAQSLHL GLPYDLPYIQ LLQTKRQERL ANLSREKIHG GILQLSSLEG IEDMVEWERL
MDLQSLDGSF LSSPASTAFV FIHTGDLKCL AFLNSVLAKF GAFVPCLYHV DLLERLLIVD
NIERLGIDRH FEKEINEALD YVYRYWSNER GIGWGRMNAT ADLETTALGF RLLRLHRYHV
SPVVFKKFKD ADGEFLSSIG QFNKDVASML NLYRACELAF PGENILDEAK GFTAKYLREA
LEKTETFSSW NIKRNLSQEI KYALKTSWHA SIPRVEAKRY CQVYRPDYAR LDKSVYKLHH
VNNEKILELA KLDFNIIQSI LQEEMKNVTS WFRDSGLPLF SFARQRPLEF YFLITAGTYE
PRYAKCRLLF TKVACVETVL DDMYDTYGTL DELKLFTQAV RRWDPSLTEN LPDYMKRCYK
IFYDIVHEAA WEAEKEQGRE LVSFLRKAWE DFVLSYHEEA EWLSAEYVPG FDEYIKNGIT
SIGQRVLLLS GLLVMDGQLL SQKALEKIDY PERSRVLMEQ ICLISRLADD TQSYKAEKAR
GELASGIECY MKDHPECTEE EALNHIYGIM EVTAKELTKE YLKVDDDDVP FACKKMLFEE
TRVTMVIFKD GDRLSNSKLE MKDHFKECLI EPLPL
