GERS_CINTE
ID GERS_CINTE Reviewed; 603 AA.
AC Q8GUE4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Geraniol synthase, chloroplastic;
DE Short=CtGES;
DE EC=3.1.7.11;
DE Flags: Precursor;
GN Name=GerS;
OS Cinnamomum tenuipile (Alseodaphne mollis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX NCBI_TaxID=192326;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND COFACTOR.
RX PubMed=15680985; DOI=10.1016/j.phytochem.2004.12.004;
RA Yang T., Li J., Wang H.-X., Zeng Y.;
RT "A geraniol-synthase gene from Cinnamomum tenuipilum.";
RL Phytochemistry 66:285-293(2005).
CC -!- FUNCTION: Monoterpene synthase that catalyzes the formation of geraniol
CC from geranyl diphosphate. {ECO:0000269|PubMed:15680985}.
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:15680985};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15680985};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15680985};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000269|PubMed:15680985};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55.8 uM for geranyl diphosphate {ECO:0000269|PubMed:15680985};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:15680985};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the oil cells of the leaves.
CC {ECO:0000269|PubMed:15680985}.
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 -!- MISCELLANEOUS: Exclusively observed in the geraniol chemotype of this
CC organism.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ457070; CAD29734.2; -; mRNA.
DR AlphaFoldDB; Q8GUE4; -.
DR SMR; Q8GUE4; -.
DR KEGG; ag:CAD29734; -.
DR BioCyc; MetaCyc:MON-12834; -.
DR BRENDA; 3.1.7.11; 12920.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0033383; P:geranyl diphosphate metabolic 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; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..603
FT /note="Geraniol synthase, chloroplastic"
FT /id="PRO_0000418927"
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"
SQ SEQUENCE 603 AA; 69081 MW; 1DF6F352C2E81745 CRC64;
MALQMIAPFL SSFLPNPRHS LAAHGLTHQK CVSKHISCST TTPTYSTTVP RRSGNYKPSI
WDYDFVQSLG SGYKVEAHGT RVKKLKEVVK HLLKETDSSL AQIELIDKLR RLGLRWLFKN
EIKQVLYTIS SDNTSIEMRK DLHAVSTRFR LLRQHGYKVS TDVFNDFKDE KGCFKPSLSM
DIKGMLSLYE ASHLAFQGET VLDEARAFVS THLMDIKENI DPILHKKVEH ALDMPLHWRL
EKLEARWYMD IYMREEGMNS SLLELAMLHF NIVQTTFQTN LKSLSRWWKD LGLGEQLSFT
RDRLVECFFW AAAMTPEPQF GRCQEVVAKV AQLIIIIDDI YDVYGTVDEL ELFTNAIDRW
DLEAMEQLPE YMKTCFLALY NSINEIGYDI LKEEGRNVIP YLRNTWTELC KAFLVEAKWY
SSGYTPTLEE YLQTSWISIG SLPMQTYVFA LLGKNLAPES SDFAEKISDI LRLGGMMIRL
PDDLGTSTDE LKRGDVPKSI QCYMHEAGVT EDVARDHIMG LFQETWKKLN EYLVESSLPH
AFIDHAMNLG RVSYCTYKHG DGFSDGFGDP GSQEKKMFMS LFAEPLQVDE AKGISFYVDG
GSA
