SSS_PICSI
ID SSS_PICSI Reviewed; 627 AA.
AC F1CKJ1; F1CKJ2;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=(+)-sabinene synthase, chloroplastic;
DE Short=SSS;
DE EC=4.2.3.110;
DE Flags: Precursor;
GN Name=TPS-sab;
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION BY METHYL JASMONATE.
RC STRAIN=H898, and Q903;
RX PubMed=21323772; DOI=10.1111/j.1365-313x.2010.04478.x;
RA Hall D.E., Robert J.A., Keeling C.I., Domanski D., Quesada A.L.,
RA Jancsik S., Kuzyk M.A., Hamberger B., Borchers C.H., Bohlmann J.;
RT "An integrated genomic, proteomic and biochemical analysis of (+)-3-carene
RT biosynthesis in Sitka spruce (Picea sitchensis) genotypes that are
RT resistant or susceptible to white pine weevil.";
RL Plant J. 65:936-948(2011).
CC -!- FUNCTION: Terpene synthase (TPS) involved in defensive oleoresin
CC formation in conifers in response to insect attack (e.g. white pine
CC weevil P.strobi) or other injury. Produces (+)-sabinene from geranyl
CC diphosphate, but has no activity with geranylgeranyl diphosphate or
CC farnesyl diphosphate. {ECO:0000269|PubMed:21323772}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (1R,5R)-sabinene + diphosphate;
CC Xref=Rhea:RHEA:32547, ChEBI:CHEBI:33019, ChEBI:CHEBI:50029,
CC ChEBI:CHEBI:58057; EC=4.2.3.110;
CC Evidence={ECO:0000269|PubMed:21323772};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.59 uM for geranyl diphosphate {ECO:0000269|PubMed:21323772};
CC Vmax=13.5 pmol/sec/ug enzyme {ECO:0000269|PubMed:21323772};
CC Note=kcat is 0.89 sec(-1) with geranyl diphosphate as substrate.;
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by methyl jasmonate.
CC {ECO:0000269|PubMed:21323772}.
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 -!- MISCELLANEOUS: The highly resistant (H898) genotype and the highly
CC susceptible (Q903) genotype differ in the nature and amount of the
CC various terpenoids found in oleoresin.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; HQ336803; ADU85929.1; -; mRNA.
DR EMBL; HQ336804; ADU85930.1; -; mRNA.
DR AlphaFoldDB; F1CKJ1; -.
DR SMR; F1CKJ1; -.
DR BRENDA; 4.2.3.110; 8974.
DR BRENDA; 4.2.3.113; 8974.
DR SABIO-RK; F1CKJ1; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; 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; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..627
FT /note="(+)-sabinene synthase, chloroplastic"
FT /id="PRO_0000419747"
FT MOTIF 378..382
FT /note="DDXXD motif"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT VARIANT 448
FT /note="E -> D (in strain: Q903; susceptible)"
FT VARIANT 463
FT /note="G -> V (in strain: Q903; susceptible)"
SQ SEQUENCE 627 AA; 71795 MW; E244D1A0411995A7 CRC64;
MSVISIVPLA SNSCLYKSLM SSTHELKALC RPIATLGMCR RGKSVMASMS TSLTTAVSDD
GVQRRIGHHH SNLWDDNFIQ SLSSPYGASS YAESAKKLIG EVKEIFNSLS MAAGGLMSPV
DDLLQHLSMV DNVERLGIDR HFQTEIKVSL DYVYSYWSEK GIGSGRDIVC TDLNTTALGF
RILRLHGYTV FPDVFEHFKD QMGRIACSAN HTERQISSIL NLFRASLIAF PGEKVMEEAE
IFSATYLKEA LQTIPVSSLS QEMQYVLDYR WHSNLPRLET RTYIDILGET TINQMQDVNI
QKLLELAKLE FNIFHSIQQN ELKCISRWWK ESGSPELTFI RHRHIEFYTL ASGIDMEPKH
SAFRLSFVKM CHLITVLDDI YDTFGTMDEL RLFTSAVKRW DRSEIECLPE YMKGVYIILY
ETVNEMAREA RKSQGRDTLN YARLALEEYI GAYLKEAEWI SMGYLPTFEE YFKNGKVSSG
HRIATLQPIL TLDIPFPHHI LQEIDFPSKF NELACSILRL RGDTRCYQAD RDRGEKASCI
SCYMKDNPGS TEEDALNHIN GMIEDTIKQL NWELLRPDNN VPISSKKHSF DISRAFHHLY
RYRDGYTVSS NETKNLVVRT VLEPLPM
