GRNL7_PERFR
ID GRNL7_PERFR Reviewed; 603 AA.
AC C0KWV6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Geraniol synthase Tps-5073G30, chloroplastic {ECO:0000303|PubMed:20447664};
DE Short=PfTps-5073G {ECO:0000303|PubMed:20447664};
DE EC=3.1.7.11 {ECO:0000269|PubMed:20447664};
DE Flags: Precursor;
GN Name=Tps-5073G30 {ECO:0000303|PubMed:20447664};
OS Perilla frutescens (Beefsteak mint) (Perilla ocymoides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Elsholtzieae; Perilla.
OX NCBI_TaxID=48386;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP COFACTOR.
RC STRAIN=cv. 5073;
RX PubMed=20447664; DOI=10.1016/j.phytochem.2010.04.006;
RA Masumoto N., Korin M., Ito M.;
RT "Geraniol and linalool synthases from wild species of perilla.";
RL Phytochemistry 71:1068-1075(2010).
CC -!- FUNCTION: Monoterpene synthase (mono-TPS) involved in the biosynthesis
CC of monoterpenes natural products (PubMed:20447664). Catalyzes the
CC conversion of (2E)-geranyl diphosphate (GPP) into geraniol
CC (PubMed:20447664). {ECO:0000269|PubMed:20447664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (2E)-geraniol + diphosphate;
CC Xref=Rhea:RHEA:32679, ChEBI:CHEBI:15377, ChEBI:CHEBI:17447,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=3.1.7.11;
CC Evidence={ECO:0000269|PubMed:20447664};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32680;
CC Evidence={ECO:0000269|PubMed:20447664};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20447664};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20447664};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:20447664}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; FJ644547; ACN42012.1; -; mRNA.
DR SMR; C0KWV6; -.
DR BRENDA; 3.1.7.11; 11839.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:1903448; P:geraniol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016099; P:monoterpenoid 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 Chloroplast; Hydrolase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 36..603
FT /note="Geraniol synthase Tps-5073G30, chloroplastic"
FT /id="PRO_0000455251"
FT MOTIF 356..360
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 360
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 504
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 508
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 603 AA; 69805 MW; E2E1F26FAF181BAF CRC64;
MCSISQKVVI GLNKAAANNN LQNLDRRGFK TRCVSSSKAA SCLRASCSLQ LDVKPAQEGR
RSGNYQPSIW DFNYVQSLNT PYKEERYLTR HAELIVQVKP LLEKKMEAAQ QLELIDDLNN
LGLSYFFQDR IKQILSFIYD ENQCFHSNIN DQAEKRDLYF TALGFKLLRQ HGFDVSQEVF
DCFKNDNGSD FKASLSDNTK GLLQLYEASF LVREGEDTLE QARQFATKFL RRKLDEIDDN
HLLSCIHHSL EIPLHWRIQR LEARWFLDAY ATRHDMNPAI LELAKLDFNI IQATHQEELK
DVSRWWQNTR LAEKLPFVRD RLVESYFWAI ALFEPHQYGY QRRVAAKIIT LATSIDDVYD
IYGTLDELQL FTDNFRRWDT ESLGIPPYSM QLFYMVIHNF VSELACEILK EKGFIVIPYL
QRSWIDLAES FLKEANWYYS GYTPSLEEYI DNGSVSIGAV AVLSQVYFTL ANSIEKPKIE
SMYKYHHILR LSGLLVRLHD DLGTSLFEKK RGDVPKAVEI CMKERNVTEE EAEEHVKYLI
REAWKEMNTA TAAAGCPFMD ELNVAAANLG RAAQFVYLDG DGHGVQHSKI HQQMGGLMFE
PYL
