TPS5_PSEAD
ID TPS5_PSEAD Reviewed; 814 AA.
AC A0A1L6Z3A5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Alpha-bisabolene synthase {ECO:0000303|PubMed:28096378};
DE EC=4.2.3.38 {ECO:0000269|PubMed:28096378};
DE AltName: Full=Terpene synthase 5 {ECO:0000303|PubMed:28096378};
DE Short=PxaTPS5 {ECO:0000303|PubMed:28096378};
GN Name=TPS5 {ECO:0000303|PubMed:28096378};
OS Pseudolarix amabilis (Golden larch) (Pseudolarix kaempferi).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC Pseudolarix.
OX NCBI_TaxID=3355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=28096378; DOI=10.1073/pnas.1612901114;
RA Mafu S., Karunanithi P.S., Palazzo T.A., Harrod B.L., Rodriguez S.M.,
RA Mollhoff I.N., O'Brien T.E., Tong S., Fiehn O., Tantillo D.J., Bohlmann J.,
RA Zerbe P.;
RT "Biosynthesis of the microtubule-destabilizing diterpene pseudolaric acid B
RT from golden larch involves an unusual diterpene synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:974-979(2017).
CC -!- FUNCTION: Converts farnesyl diphosphate to alpha-bisabolene
CC (PubMed:28096378). Involved in defensive oleoresin formation in
CC conifers in response to insect attack or other injury (By similarity).
CC Involved in sesquiterpene (C15) olefins biosynthesis (By similarity).
CC {ECO:0000250|UniProtKB:O81086, ECO:0000269|PubMed:28096378}.
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 Evidence={ECO:0000269|PubMed:28096378};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25437;
CC Evidence={ECO:0000269|PubMed:28096378};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O81086};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O81086};
CC Note=Binds 3 divalent metal cations per subunit. Can use either Mg(2+)
CC or Mn(2+). {ECO:0000250|UniProtKB:O81086};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in young and mature roots.
CC {ECO:0000269|PubMed:28096378}.
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; KU685113; APT40485.1; -; mRNA.
DR AlphaFoldDB; A0A1L6Z3A5; -.
DR SMR; A0A1L6Z3A5; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0052681; F:alpha-bisabolene synthase activity; IEA:UniProtKB-EC.
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 Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..814
FT /note="Alpha-bisabolene synthase"
FT /id="PRO_0000450340"
FT MOTIF 563..567
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 563
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 563
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 567
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 567
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 710
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 714
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81086"
FT BINDING 718
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O81086"
SQ SEQUENCE 814 AA; 93272 MW; 833640C82BE6CFC4 CRC64;
MAGVSVESKV SSLVCNLSST SGLIRRTANP HPNVWGYDFV HSLKSPYTDS SYRERADALV
VEIKAMLNAA IAGDGESTIT PSAYDTAWVA RVPAIDGSAR PQFPQTVDWI LKNQLKDGSW
GIESHFLLSD RLLATLSCVI ALFKWNVGDL QVKQGIEFIK SNLELVKDES DQDSLVTDFE
IIFPSLLREA QSLSLELPYD LPYIHLLQTK RQERLAKVSR EEIYTVPSPL LYSLEGIQDI
VEWDRIMDVQ GQDGSFLSSP ASTACVFIDV KCLEFLNNVM MKLGNFVPCL YPVDLLERLL
IVDNIERLGI YRHFEKEINE ALDYVYRHWN ERGIGWGTRN PIADLETTAL GFLLLRLHRY
NVSPAVFDNF KDSNGQFFCS TGQLNKDVAS MLSLYRASQL AFPGEDILDE AKSFTTKYLR
EALEKSETSS AWNNKQNLSQ EIKYALKTSW HASVARVEAK RYCQVYRPDY ARLAKSVYRL
PYVNNEKFLE LGKLDFNIIQ AIHQEEMKTV TSWFRDSGLP LFTFARERPL EFYFLVATGT
YEPQYAKCRF LFTKVACLQT VLDDMYDTYG TLDELKLFTE AVRRWDLSFT ENLPDYMKLC
YKIYYDIVHE VAWEAEKEQG RELVSFFRKG WEDYLLGYYE EAEWLASEYV PSLDEYIKNG
ITSIGQRILL LSGVLIMDGQ LLSQEALEKV DYPGRRVLTE LNSLISRLAD DTKTYKAEKA
RGELASSIEC YMKDHPECTE EEALAHIYSI LEPAVKELTR EFLKPDDVPF ACKKMLFEET
RVTMVIFKDG DGFGVSKLEV KDHIKESLID PLPL
