ISOPS_PICSI
ID ISOPS_PICSI Reviewed; 874 AA.
AC F2XF92;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Isopimaradiene synthase, chloroplastic {ECO:0000303|PubMed:21385377};
DE EC=4.2.3.- {ECO:0000269|PubMed:21385377};
DE AltName: Full=Terpene synthase TPS-Iso {ECO:0000303|PubMed:21385377};
DE Short=PsTPS-Iso {ECO:0000303|PubMed:21385377};
DE Flags: Precursor;
GN Name=TPS-Iso {ECO:0000303|PubMed:21385377};
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], CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND GENE
RP FAMILY.
RC STRAIN=cv. Haney 898;
RX PubMed=21385377; DOI=10.1186/1471-2229-11-43;
RA Keeling C.I., Weisshaar S., Ralph S.G., Jancsik S., Hamberger B.,
RA Dullat H.K., Bohlmann J.;
RT "Transcriptome mining, functional characterization, and phylogeny of a
RT large terpene synthase gene family in spruce (Picea spp.).";
RL BMC Plant Biol. 11:43-43(2011).
CC -!- FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of
CC diterpene natural products included in conifer oleoresin secretions and
CC volatile emissions; these compounds contribute to biotic and abiotic
CC stress defense against herbivores and pathogens (PubMed:21385377).
CC Catalyzes the conversion of (+)-copalyl diphosphate ((+)-CPP) to
CC isopimaradiene (PubMed:21385377). {ECO:0000269|PubMed:21385377}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = diphosphate + isopimara-8(14),15-
CC diene; Xref=Rhea:RHEA:32003, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635,
CC ChEBI:CHEBI:63708; Evidence={ECO:0000269|PubMed:21385377};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:21385377}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC activity in the class II active site relevant for the cyclization of
CC GGPP. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the
CC catalytic activity in the class I active site, presumably through
CC binding to Mg(2+). {ECO:0000250|UniProtKB:A0A1C9J6A7,
CC ECO:0000250|UniProtKB:A9AWD5}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; HQ426150; ADZ45512.1; -; mRNA.
DR OMA; ENGAFIC; -.
DR UniPathway; UPA00924; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
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 Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..37
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 38..874
FT /note="Isopimaradiene synthase, chloroplastic"
FT /id="PRO_0000454418"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 407..410
FT /note="DXDD motif"
FT /evidence="ECO:0000250|UniProtKB:A9AWD5"
FT MOTIF 626..630
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 407
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 409
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 626
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 626
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 630
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 630
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 770
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 778
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 874 AA; 100218 MW; C73F4D60A62996FF CRC64;
MALPSSSLSS RIPTGPHPLT HTQCIPHFST TINAGISAAK PRSFYLRWGK DSQPKNLGSN
KIIACVGEGT TSLPYQSAEK TDSLSAPTLV KREFPPGFWK DHVIDSLTSS HKVSAAEEKR
IETLISDIKN IFRSMGYGET NPSAYDTAWV ARIPAVDGSE QPEFPETLEW ILQNQLKDGS
WGEGFYFLAY DRILATLACM ITLTLWRTGE TQIRKGIEFF KTQAGKIEDE ADSHRPSGFE
IVFPAMLKEA KVLGLDLPYE LSFIKQIIEK REAKLERLPT NILYALPTTL LYSLEGLQEI
VDWQKIIKLQ SKDGSFLTSP ASTAAVFMRT GNKKCLEFLN FVLKKFGNHV PCHYPLDLFE
RLWAVDTVER LGIDRHFKEE IKDALDYVYS HWDERGIGWA RENPVPDIDD TAMGLRILRL
HGYNVSSDVL KTFRDENGEF FCFLGQTQRG VTDMLNVNRC SHVAFPGETI MQEAKLCTER
YLRNALEDVG AFDKWALKKN IRGEVEYALK YPWHRSMPRL EARSYIEHYG PNDVWLGKTM
YMMPYISNEK YLELAKLDFN HVQSLHQKEL RDLRRWWKSS GFSDLKFTRE RVTEIYFSAA
SFIFEPEFAT CRYVYTKMSI FTVILDDLYD AHGTLDNLNL FSEGVKRWDL SLVDRMPQDM
KICFTVLYNT VNEIAVEGRK RQGRDVLGYI RNVLEILLAA HTKEAEWSAT RYVPSFDEYI
ENASVSISLG TVVLISALFT GEILTDDVLS KIGRGSRFLQ LMDLTGRLVN DTKTYQAERG
QGEVASAVQC YMKDHPEISE EEALKHVYTV MENALDELNR EFVNNREVPD SCRRLVFETA
RIMQWFYMEG DGFTVSHEME IKEHVKNCLF QPVA
