TPS1_ANTMA
ID TPS1_ANTMA Reviewed; 579 AA.
AC Q84NC8;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Tricyclene synthase 0e23, chloroplastic;
DE Short=Am0e23;
DE EC=4.2.3.105;
DE AltName: Full=(E)-beta-ocimene synthase 0e23;
DE EC=4.2.3.106;
DE AltName: Full=Terpenoid synthase 0e23;
DE Flags: Precursor;
GN Name=0e23;
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 INDUCTION.
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 = (E)-beta-ocimene + diphosphate;
CC Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:64280; EC=4.2.3.106;
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. {ECO:0000269|PubMed:12724546}.
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; AY195607; AAO42614.1; -; mRNA.
DR AlphaFoldDB; Q84NC8; -.
DR SMR; Q84NC8; -.
DR PRIDE; Q84NC8; -.
DR KEGG; ag:AAO42614; -.
DR BRENDA; 4.2.3.106; 376.
DR UniPathway; UPA00213; -.
DR GO; GO:0009570; C:chloroplast stroma; ISS:UniProtKB.
DR GO; GO:0034768; F:(E)-beta-ocimene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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..66
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 67..579
FT /note="Tricyclene synthase 0e23, chloroplastic"
FT /id="PRO_0000418161"
FT MOTIF 336..340
FT /note="DDXXD motif"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 488
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 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 579 AA; 66728 MW; 3A751DA86877145C CRC64;
MAFCISYLGA VLPFSLSPRT KFAIFHNTSK HAAYKTCRWN IPRDVGSTPP PSKLHQALCL
NAHSTSCMAE LPMDYEGKIQ GTRHLLHLKD ENDPIESLIF VDATQRLGVN HHFQKEIEEI
LRKSYATMKS PSICKYHTLH DVSLFFCLMR QHGRYVSADV FNNFKGESGR FKEELKRDTR
GLVELYEAAQ LSFEGERILD EAENFSRQIL HGNLASMEDN LRRSVGNKLR YPFHKSIARF
TGINYDDDLG GMYEWGKTLR ELALMDLQVE RSVYQEELLQ VSKWWNELGL YKKLTLARNR
PFEFYMWSMV ILTDYINLSE QRVELTKSVA FIYLIDDIFD VYGTLDELII FTEAVNKWDY
SATDTLPDNM KMCYMTLLDT INGTSQKIYE KYGHNPIDSL KTTWKSLCSA FLVEAKWSAS
GSLPSANEYL ENEKVSSGVY VVLIHLFFLM GLGGTNRGSI ELNDTRELMS SIAIIVRIWN
DLGCAKNEHQ NGKDGSYLDC YKKEHINLTA AQVHEHALEL VAIEWKRLNK ESFNLNHDSV
SSFKQAALNF ARMVPLMYSY DNNRRGPVLE EYVKFMLSD
