TPS2_ANTMA
ID TPS2_ANTMA Reviewed; 581 AA.
AC Q84ND0;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Tricyclene synthase Oc15, chloroplastic;
DE Short=AmOc15;
DE EC=4.2.3.105;
DE AltName: Full=Myrcene synthase Oc15;
DE EC=4.2.3.15;
DE AltName: Full=Terpenoid synthase Oc15;
DE Flags: Precursor;
GN Name=Oc15;
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, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, CATALYTIC ACTIVITY, AND
RP 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: Contributes 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 in flowers; mostly expressed in both
CC upper and lower petal lobes, and, to a lower extent, in tube and
CC 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 levels 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; AY195608; AAO41726.1; -; mRNA.
DR AlphaFoldDB; Q84ND0; -.
DR SMR; Q84ND0; -.
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; IDA:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0102701; F:tricyclene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
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..68
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 69..581
FT /note="Tricyclene synthase Oc15, chloroplastic"
FT /id="PRO_0000418162"
FT MOTIF 338..342
FT /note="DDXXD motif"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 490
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 581 AA; 66705 MW; 71A795B10A46359C CRC64;
MAFCISYVGA LLPCSLSTRT KFAICHNTSK LHRAAYKTSR WNIPGDVGST PPPSKLHQAL
CLNEHSLSCM AELPMDYEGK IKETRHLLHL KGENDPIESL IFVDATLRLG VNHHFQKEIE
EILRKSYATM KSPIICEYHT LHEVSLFFRL MRQHGRYVSA DVFNNFKGES GRFKEELKRD
TRGLVELYEA AQLSFEGERI LDEAENFSRQ ILHGNLAGME DNLRRSVGNK LRYPFHTSIA
RFTGRNYDDD LGGMYEWGKT LRELALMDLQ VERSVYQEEL LQVSKWWNEL GLYKKLNLAR
NRPFEFYTWS MVILADYINL SEQRVELTKS VAFIYLIDDI FDVYGTLDEL IIFTEAVNKW
DYSATDTLPE NMKMCCMTLL DTINGTSQKI YEKHGYNPID SLKTTWKSLC SAFLVEAKWS
ASGSLPSANE YLENEKVSSG VYVVLVHLFC LMGLGGTSRG SIELNDTQEL MSSIAIIFRL
WNDLGSAKNE HQNGKDGSYL NCYKKEHINL TAAQAHEHAL ELVAIEWKRL NKESFNLNHD
SVSSFKQAAL NLARMVPLMY SYDHNQRGPV LEEYVKFMLS D