GTPS_CITLI
ID GTPS_CITLI Reviewed; 600 AA.
AC Q8L5K4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Gamma-terpinene synthase, chloroplastic;
DE Short=ClgammaTS;
DE EC=4.2.3.114;
DE Flags: Precursor;
OS Citrus limon (Lemon) (Citrus medica var. limon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Peelings;
RX PubMed=12084056; DOI=10.1046/j.1432-1033.2002.02985.x;
RA Lucker J., El Tamer M.K., Schwab W., Verstappen F.W.A.,
RA van der Plas L.H.W., Bouwmeester H.J., Verhoeven H.A.;
RT "Monoterpene biosynthesis in lemon (Citrus limon): cDNA isolation and
RT functional analysis of four monoterpene synthases.";
RL Eur. J. Biochem. 269:3160-3171(2002).
CC -!- FUNCTION: Monoterpene synthase which catalyzes the conversion of
CC geranyl diphosphate to gamma-terpinene and the minor products limonene,
CC alpha-pinene, beta-pinene, alpha-terpinolene, alpha-thujene, alpha-
CC terpinene, myrcene and sabinene. {ECO:0000269|PubMed:12084056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene;
CC Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.114;
CC Evidence={ECO:0000269|PubMed:12084056};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12084056};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12084056};
CC Note=Manganese > magnesium. {ECO:0000269|PubMed:12084056};
CC -!- ACTIVITY REGULATION: Inhibited by 100 mM KCl.
CC {ECO:0000269|PubMed:12084056}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.7 uM for geranyl diphosphate {ECO:0000269|PubMed:12084056};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:12084056};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AF514286; AAM53943.1; -; mRNA.
DR AlphaFoldDB; Q8L5K4; -.
DR SMR; Q8L5K4; -.
DR PRIDE; Q8L5K4; -.
DR KEGG; ag:AAM53943; -.
DR BRENDA; 4.2.3.114; 1413.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0102903; F:gamma-terpinene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
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; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 41..600
FT /note="Gamma-terpinene synthase, chloroplastic"
FT /id="PRO_0000418652"
FT MOTIF 353..357
FT /note="DDXXD motif"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 600 AA; 69522 MW; 2EABD0C9DEE2CAE8 CRC64;
MALNLLSSLP AACNFTRLSL PLSSKVNGFV PPITQVQYPM AASTSSIKPV DQTIIRRSAD
YGPTIWSFDY IQSLDSKYKG ESYARQLEKL KEQVSAMLQQ DNKVVDLDPL HQLELIDNLH
RLGVSYHFED EIKRTLDRIH NKNTNKSLYA RALKFRILRQ YGYKTPVKET FSRFMDEKGS
FKLSSHSDEC KGMLALYEAA YLLVEEESSI FRDAIRFTTA YLKEWVAKHD IDKNDNEYLC
TLVKHALELP LHWRMRRLEA RWFIDVYESG PDMNPILLEL AKVDYNIVQA VHQEDLKYVS
RWWKKTGLGE KLNFARDRVV ENFFWTVGDI FEPQFGYCRR MSAMVNCLLT SIDDVYDVYG
TLDELELFTD AVERWDATTT EQLPYYMKLC FHALYNSVNE MGFIALRDQE VGMIIPYLKK
AWADQCKSYL VEAKWYNSGY IPTLQEYMEN AWISVTAPVM LLHAYAFTAN PITKEALEFL
QDSPDIIRIS SMIVRLEDDL GTSSDELKRG DVPKSIQCYM HETGVSEDEA REHIRDLIAE
TWMKMNSARF GNPPYLPDVF IGIAMNLVRM SQCMYLYGDG HGVQENTKDR VLSLFIDPIP
