GERS_OCIBA
ID GERS_OCIBA Reviewed; 567 AA.
AC Q6USK1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Geraniol synthase, chloroplastic;
DE Short=ObGES;
DE EC=3.1.7.11;
DE Flags: Precursor;
GN Name=GES;
OS Ocimum basilicum (Sweet basil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Ociminae;
OC Ocimum.
OX NCBI_TaxID=39350;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. SD; TISSUE=Peltate glandular trichome;
RX PubMed=14657409; DOI=10.1104/pp.103.032946;
RA Iijima Y., Gang D.R., Fridman E., Lewinsohn E., Pichersky E.;
RT "Characterization of geraniol synthase from the peltate glands of sweet
RT basil.";
RL Plant Physiol. 134:370-379(2004).
CC -!- FUNCTION: Monoterpene synthase that catalyzes the formation of geraniol
CC from geranyl diphosphate. {ECO:0000269|PubMed:14657409}.
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:14657409};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:14657409};
CC Note=Binds 3 Mn(2+) ions per subunit. {ECO:0000269|PubMed:14657409};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for geranyl diphosphate {ECO:0000269|PubMed:14657409};
CC KM=51 uM for Mn(2+) {ECO:0000269|PubMed:14657409};
CC Vmax=6.244 pmol/sec/mg enzyme {ECO:0000269|PubMed:14657409};
CC Note=kcat is 0.8 sec(-1) with geranyl diphosphate as substrate.
CC {ECO:0000269|PubMed:14657409};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:14657409};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14657409}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the peltate glandular trichomes of the
CC leaves. {ECO:0000269|PubMed:14657409}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY362553; AAR11765.1; -; mRNA.
DR AlphaFoldDB; Q6USK1; -.
DR SMR; Q6USK1; -.
DR KEGG; ag:AAR11765; -.
DR BioCyc; MetaCyc:MON-13787; -.
DR BRENDA; 3.1.7.11; 4385.
DR SABIO-RK; Q6USK1; -.
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; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA: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; Manganese; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..567
FT /note="Geraniol synthase, chloroplastic"
FT /id="PRO_0000418928"
FT REGION 48..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 323..327
FT /note="DDXXD motif"
FT COMPBIAS 60..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 323
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 567 AA; 64933 MW; 9D3A9ED51FA52B93 CRC64;
MSCARITVTL PYRSAKTSIQ RGITHYPALI RPRFSACTPL ASAMPLSSTP LINGDNSQRK
NTRQHMEESS SKRREYLLEE TTRKLQRNDT ESVEKLKLID NIQQLGIGYY FEDAINAVLR
SPFSTGEEDL FTAALRFRLL RHNGIEISPE IFLKFKDERG KFDESDTLGL LSLYEASNLG
VAGEEILEEA MEFAEARLRR SLSEPAAPLH GEVAQALDVP RHLRMARLEA RRFIEQYGKQ
SDHDGDLLEL AILDYNQVQA QHQSELTEII RWWKELGLVD KLSFGRDRPL ECFLWTVGLL
PEPKYSSVRI ELAKAISILL VIDDIFDTYG EMDDLILFTD AIRRWDLEAM EGLPEYMKIC
YMALYNTTNE VCYKVLRDTG RIVLLNLKST WIDMIEGFME EAKWFNGGSA PKLEEYIENG
VSTAGAYMAF AHIFFLIGEG VTHQNSQLFT QKPYPKVFSA AGRILRLWDD LGTAKEEQER
GDLASCVQLF MKEKSLTEEE ARSRILEEIK GLWRDLNGEL VYNKNLPLSI IKVALNMARA
SQVVYKHDQD TYFSSVDNYV DALFFTQ
