TPS3_ANTMA
ID TPS3_ANTMA Reviewed; 584 AA.
AC Q84NC9;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Tricyclene synthase 1e20, chloroplastic;
DE Short=Am1e20;
DE EC=4.2.3.105;
DE AltName: Full=Myrcene synthase 1e20;
DE EC=4.2.3.15;
DE AltName: Full=Terpenoid synthase 1e20;
DE Flags: Precursor;
GN Name=1e20;
OS Antirrhinum majus (Garden snapdragon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX NCBI_TaxID=4151;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, CATALYTIC ACTIVITY, AND CIRCADIAN-REGULATION.
RC TISSUE=Petal;
RX PubMed=12724546; DOI=10.1105/tpc.011015;
RA Dudareva N., Martin D., Kish C.M., Kolosova N., Gorenstein N., Faeldt J.,
RA Miller B., Bohlmann J.;
RT "(E)-beta-ocimene and myrcene synthase genes of floral scent biosynthesis
RT in snapdragon: function and expression of three terpene synthase genes of a
RT new terpene synthase subfamily.";
RL Plant Cell 15:1227-1241(2003).
CC -!- FUNCTION: May contribute to floral scent emission.
CC {ECO:0000269|PubMed:12724546}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + tricyclene;
CC Xref=Rhea:RHEA:32687, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:64266; EC=4.2.3.105;
CC Evidence={ECO:0000269|PubMed:12724546};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.15;
CC Evidence={ECO:0000269|PubMed:12724546};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Accumulates at low levels in flowers; mostly
CC expressed in both upper and lower petal lobes, and, to a lower extent,
CC in tube and stamens. {ECO:0000269|PubMed:12724546}.
CC -!- DEVELOPMENTAL STAGE: First observed in mature flower buds and
CC accumulates transiently during 4 days after anthesis.
CC {ECO:0000269|PubMed:12724546}.
CC -!- INDUCTION: Circadian-regulation with highest levels in early afternoon
CC and lowest level during the night.
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 -!- SIMILARITY: Belongs to the terpene synthase family. Tpsg subfamily.
CC {ECO:0000305}.
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DR EMBL; AY195609; AAO41727.1; -; mRNA.
DR AlphaFoldDB; Q84NC9; -.
DR SMR; Q84NC9; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009570; C:chloroplast stroma; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050551; F:myrcene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0010333; F:terpene synthase activity; ISS:UniProtKB.
DR GO; GO:0102701; F:tricyclene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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; Glycoprotein; Lyase; Magnesium; Manganese; Metal-binding;
KW Plastid; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..584
FT /note="Tricyclene synthase 1e20, chloroplastic"
FT /id="PRO_0000418163"
FT MOTIF 341..345
FT /note="DDXXD motif"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 584 AA; 67339 MW; 1D21C002FF060FE7 CRC64;
MIYIWICFYL QTTLLPCSLS TRTKFAICHN TSKLHRAAYK TSRWNIPGDV GSTPPPSKLH
QALCLNEHSL SCMAELPMDY EGKIKETRHL LHLKGENDPI ESLIFVDATL RLGVNHHFQK
EIEEILRKSY ATMKSPIICE YHTLHEVSLF FRLMRQHGRY VSADVFNNFK GESGRFKEEL
KRDTRGLVEL YEAAQLSFEG ERILDEAENF SRQILHGNLA GMEDNLRRSV GNKLRYPFHT
SIARFTGRNY DDDLGGMYEW GKTLRELALM DLQVERSVYQ EELLQVSKWW NELGLYKKLN
LARNRPFEFY TWSMVILADY INLSEQRVEL TKSVAFIYLI DDIFDVYGTL DELIIFTEAV
NKWDYSATDT LPENMKMCCM TLLDTINGTS QKIYEKHGYN PIDSLKTTWK SLCSAFLVEA
KWSASGSLPS ANEYLENEKV SSGVYVVLVH LFCLMGLGGT SRGSIELNDT QELMSSIAII
FRLWNDLGSA KNEHQNGKDG SYLNCYKKEH INLTAAQAHE HALELVAIEW KRLNKESFNL
NHDSVSSFKQ AALNLARMVP LMYSYDHNQR GPVLEEYVKF MLSD
