TPSLS_PICAB
ID TPSLS_PICAB Reviewed; 578 AA.
AC Q675L0; Q94KA3;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Longifolene synthase;
DE Short=PaTPS-Lon;
DE EC=4.2.3.58;
GN Name=TPS-Lon;
OS Picea abies (Norway spruce) (Picea excelsa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3329;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Morency M.J., Nicole M.C., Seguin A.;
RT "Terpene synthase from Norway spruce, cDNA isolation and characterization
RT for gamma-humulene synthase-like gene by 5'-and 3'-RACE amplification.";
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=15310829; DOI=10.1104/pp.104.042028;
RA Martin D.M., Faeldt J., Bohlmann J.;
RT "Functional characterization of nine Norway Spruce TPS genes and evolution
RT of gymnosperm terpene synthases of the TPS-d subfamily.";
RL Plant Physiol. 135:1908-1927(2004).
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 longifolene, but also
CC multiple minor products including alpha-longipinene, alpha-
CC longicyclene, E-beta-farnesene, longiborneol, cyclosativene, beta-
CC longipinene, and 12 other sesquiterpenes when used with farnesyl
CC diphosphate (FPP) as substrate. {ECO:0000269|PubMed:15310829}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + longifolene;
CC Xref=Rhea:RHEA:25464, ChEBI:CHEBI:6530, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.58;
CC Evidence={ECO:0000269|PubMed:15310829};
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:15310829}.
CC -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC {ECO:0000269|PubMed:15310829}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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}.
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; AF369920; AAK39129.2; -; mRNA.
DR EMBL; AY473625; AAS47695.1; -; mRNA.
DR AlphaFoldDB; Q675L0; -.
DR SMR; Q675L0; -.
DR KEGG; ag:AAS47695; -.
DR BioCyc; MetaCyc:MON-12770; -.
DR BRENDA; 4.2.3.58; 4815.
DR BRENDA; 4.2.3.80; 4815.
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 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 Cytoplasm; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..578
FT /note="Longifolene synthase"
FT /id="PRO_0000412237"
FT MOTIF 331..335
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 210
FT /note="N -> D (in Ref. 1; AAK39129)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="W -> C (in Ref. 1; AAK39129)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="S -> A (in Ref. 1; AAK39129)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="Missing (in Ref. 1; AAK39129)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 67181 MW; ED8146674FF126C9 CRC64;
MAQISKCSSL SAELNESSII SHHHGNLWDD DFIQSLKSSN GAPQYHERAA KLVEEIKNLV
VSEMKDCNDD LIRRLQMVDI FECLGIDRHF QHEIQVALDY VYRYWNQLEG IGIGSRDSLI
KDFNATALGF RALRLHRYNV SSDVLENFKN ENGQFFCSST VEEKEVRCML TLFRASEISF
PGEKVMDEAK AFTTEYLTKV LTGVDVTDVN QSLLREVKYA LEFPWHCSLP RWEARSFIEI
CGQNDSWLKS IMNKRVLELA KLDFNILQWA HHRELQLLSS WWSQSDIAQQ NFYRKRHVEF
YLWVVIGTFE PEFSTCRITF AKISTLMTIL DDLYDTHGTL EQLKIFTEGV KRWDLSLVDR
LPDYIKITFE FFLNTSNELI AEVAKTQERD MSAYIRKTWE RYLEAYLQEA EWIAARHVPT
FDEYMKNGIS SSGMCILNLY SLLLMGQLLP DDVLEQIHSP SKIHELVELT ARLVDDSKDF
ETKKVGGELA SGIECYVKDN PECTLEDASN HLNGLLDLTV KELNWEFVRH DSVALCFKKF
AFNVARGLRL IYKYRDGFDV SNQEMKTHIF KILIDPLT
