GRNLC_PERFH
ID GRNLC_PERFH Reviewed; 603 AA.
AC Q4JHG3;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Geraniol synthase, chloroplastic {ECO:0000303|PubMed:17187833};
DE Short=PcTps-C {ECO:0000303|PubMed:17187833};
DE EC=3.1.7.11 {ECO:0000269|PubMed:17187833};
DE Flags: Precursor;
GN Name=Tps-C {ECO:0000303|PubMed:17187833};
OS Perilla frutescens var. hirtella (Perilla citriodora) (Perilla setoyensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Elsholtzieae; Perilla.
OX NCBI_TaxID=608512;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP COFACTOR.
RC STRAIN=cv. 1861, cv. 4935, and cv. 87; TISSUE=Leaf;
RX PubMed=17187833; DOI=10.1016/j.phytochem.2006.11.006;
RA Ito M., Honda G.;
RT "Geraniol synthases from perilla and their taxonomical significance.";
RL Phytochemistry 68:446-453(2007).
CC -!- FUNCTION: Monoterpene synthase (mono-TPS) involved in the biosynthesis
CC of monoterpenes natural products (PubMed:17187833). Catalyzes the
CC conversion of (2E)-geranyl diphosphate (GPP) into geraniol
CC (PubMed:17187833). {ECO:0000269|PubMed:17187833}.
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:17187833};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32680;
CC Evidence={ECO:0000269|PubMed:17187833};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17187833};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17187833};
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:17187833}.
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; DQ088667; AAY88965.1; -; mRNA.
DR EMBL; DQ234298; ABB30216.1; -; mRNA.
DR EMBL; DQ234299; ABB30217.1; -; mRNA.
DR SMR; Q4JHG3; -.
DR BioCyc; MetaCyc:MON-13790; -.
DR BRENDA; 3.1.7.11; 12918.
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; 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 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, chloroplastic"
FT /id="PRO_0000455254"
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; 70035 MW; 2A01A564C2EDF730 CRC64;
MSSISQKVVI GLNKAAANNN LQNLDRRGFK TRCVSSSKAA SCLRASCSLQ LDVKPVQEGR
RSGNYQPSIW DFNYVQSLNT PYKEERYLTR HAELIVQVKP LLEKKMEPAQ QLELIDDLNN
LGLSYFFQDR IKQILSFIYD ENQCFHSNIN DQAEKRDLYF TALGFRLLRQ HGFDVSQEVF
DCFKNDNGSD FKASLSDNTK GLLQLYEASF LVREGEDTLE QARQFATKFL RRKLDEIDDN
HLLSCIHHSL EIPLHWRIQR LEARWFLDAY ATRHDMNPVI LELAKLDFNI IQATHQEELK
DVSRWWQNTR LAEKLPFVRD RLVESYFWAI ALFEPHQYGY QRRVAAKIIT LATSIDDVYD
IYGTLDELQL FTDNFRRWDT ESLGRLPYSM QLFYMVIHNF VSELAYEILK EKGFIVIPYL
QRSWVDLAES FLKEANWYYS GYTPSLEEYI DNGSISIGAV AVLSQVYFTL ANSIEKPKIE
SMYKYHHILR LSGLLVRLHD DLGTSLFEKK RGDVPKAVEI CMKERNVTEE EAEEHVKYLI
REAWKEMNTA TTAAGCPFMD ELNVAAANLG RAAQFVYLDG DGHGVQHSKI HQQMGGLMFE
PYV
