ALGPS_PICSI
ID ALGPS_PICSI Reviewed; 579 AA.
AC C0PPM5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Alpha-longipinene synthase {ECO:0000303|PubMed:21385377};
DE EC=4.2.3.80 {ECO:0000269|PubMed:21385377};
DE AltName: Full=Terpene synthase TPS-Lonp {ECO:0000303|PubMed:21385377};
DE Short=PsTPS-Lonp {ECO:0000303|PubMed:21385377};
GN Name=TPS-Lonp {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 [LARGE SCALE MRNA].
RC STRAIN=cv. FB3-425; TISSUE=Green leaf;
RX PubMed=18854048; DOI=10.1186/1471-2164-9-484;
RA Ralph S.G., Chun H.J.E., Kolosova N., Cooper D., Oddy C., Ritland C.E.,
RA Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J.M., Marra M.A.,
RA Douglas C.J., Ritland K., Bohlmann J.;
RT "A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464
RT high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea
RT sitchensis).";
RL BMC Genomics 9:484-484(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PATHWAY, AND GENE
RP FAMILY.
RC STRAIN=cv. FB3-425;
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 sesquiterpene natural products included in conifer oleoresin secretions
CC and volatile emissions; these compounds contribute to biotic and
CC abiotic stress defense against herbivores and pathogens
CC (PubMed:21385377). Catalyzes the conversion of (2E,6E)-farnesyl
CC diphosphate (FPP) to alpha-longipinene (PubMed:21385377).
CC {ECO:0000269|PubMed:21385377}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-longipinene +
CC diphosphate; Xref=Rhea:RHEA:31439, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:62753, ChEBI:CHEBI:175763; EC=4.2.3.80;
CC 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: Sesquiterpene biosynthesis. {ECO:0000269|PubMed:21385377}.
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:21385377}.
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|UniProtKB:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC {ECO:0000305}.
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DR EMBL; BT070245; ACN39765.1; -; mRNA.
DR EMBL; HQ426161; ADZ45516.1; -; mRNA.
DR OMA; CAHHREL; -.
DR UniPathway; UPA00924; -.
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; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016106; P:sesquiterpenoid 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; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..579
FT /note="Alpha-longipinene synthase"
FT /id="PRO_0000454416"
FT MOTIF 332..336
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 579 AA; 67228 MW; E694028FA7047256 CRC64;
MAQISKCSSL STELNESSII SHHHGNLWDD DFIQSLKSSN GAPQYHERAE KLVEEIKNLV
VSEMKDCNDD LIRHLQMVDI FECLGIDRHF QNEIQVALDY VYRYWNELEG IGIGSRDSLI
KDFNATALGF RALRLHRYNV SSDVLENFKN ENGQFFCSST VEEKEVRCML TLFRASEISF
PGEKVMDEAK AFTTEYLTKV LTGVDVTDVD QSLLREVKYA LEFPWHCSLP RWEARNFIEI
CGQNDSWLKS IMNKRVLELA KLDFNILQCA HHRELQLLSR CWWSQSDIAQ QNFYRKRHVE
FYFWVVIGTF EPEFSTCRIT FAKIATLMTI LDDLYDTHGT LEQLKIFTEG VKRWDLSLVD
SLPDYIKITF EFFLNTSNEL IAEVAKTQER DMSAYIRKTW ERYLEAYMQE AEWITAGHVP
TFDEYMKNGI SSSGMCILNL YSLLLMGQLL PDDVLEQIHS PSKIHELVEL TARLVDDSKD
FETNKVGGEL ASGIECYVKD NPECTLEDAS NHLNGLLDLT VKELNWEFVR HDSVALCFKK
FAFNVARGLR LIYKYRDGFD VSNQEMKTHI FKILIDPLT
