PHS1_SOLLC
ID PHS1_SOLLC Reviewed; 778 AA.
AC C1K5M3;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Beta-phellandrene synthase (neryl-diphosphate-cyclizing), chloroplastic;
DE EC=4.2.3.51;
DE Flags: Precursor;
GN Name=PHS1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=19487664; DOI=10.1073/pnas.0904113106;
RA Schilmiller A.L., Schauvinhold I., Larson M., Xu R., Charbonneau A.L.,
RA Schmidt A., Wilkerson C., Last R.L., Pichersky E.;
RT "Monoterpenes in the glandular trichomes of tomato are synthesized from a
RT neryl diphosphate precursor rather than geranyl diphosphate.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:10865-10870(2009).
CC -!- FUNCTION: Monoterpene synthase catalyzing the production of beta-
CC phellandrene from neryl diphosphate. Produces also lower amounts of
CC delta-2-carene, alpha-phellandrene and limonene. When incubated in
CC vitro with geranyl diphosphate, catalyzes the formation of acyclic
CC myrcene and ocimene as major products in addition to beta-phellandrene.
CC {ECO:0000269|PubMed:19487664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=neryl diphosphate = beta-phellandrene + diphosphate;
CC Xref=Rhea:RHEA:27830, ChEBI:CHEBI:33019, ChEBI:CHEBI:48741,
CC ChEBI:CHEBI:57665; EC=4.2.3.51;
CC Evidence={ECO:0000269|PubMed:19487664};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.1 uM for neryl diphosphate {ECO:0000269|PubMed:19487664};
CC KM=2900 uM for geranyl diphosphate {ECO:0000269|PubMed:19487664};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Trichomes. {ECO:0000269|PubMed:19487664}.
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. Tpse subfamily.
CC {ECO:0000305}.
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DR EMBL; FJ797957; ACO56896.1; -; mRNA.
DR RefSeq; NP_001234629.1; NM_001247700.1.
DR AlphaFoldDB; C1K5M3; -.
DR SMR; C1K5M3; -.
DR STRING; 4081.Solyc08g005670.2.1; -.
DR PaxDb; C1K5M3; -.
DR PRIDE; C1K5M3; -.
DR GeneID; 100316883; -.
DR KEGG; sly:100316883; -.
DR eggNOG; ENOG502SI1N; Eukaryota.
DR InParanoid; C1K5M3; -.
DR OrthoDB; 247204at2759; -.
DR BioCyc; MetaCyc:MON-15450; -.
DR BRENDA; 4.2.3.51; 3101.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; C1K5M3; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0010333; F:terpene synthase activity; IBA:GO_Central.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
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; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..778
FT /note="Beta-phellandrene synthase (neryl-diphosphate-
FT cyclizing), chloroplastic"
FT /id="PRO_0000405121"
FT MOTIF 531..535
FT /note="DDXXD motif"
FT BINDING 531
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 531
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 676
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 778 AA; 90819 MW; DFC318D00DB171E5 CRC64;
MIVGYRSTII TLSHPKLGNG KTISSNAIFQ RSCRVRCSHS TTSSMNGFED ARDRIRESFG
KLELSPSSYD TAWVAMVPSR HSLNEPCFPQ CLDWIIENQR EDGSWGLNPT HPLLLKDSLS
STLACLLALT KWRVGDEQIK RGLGFIETYG WAVDNKDQIS PLGFEVIFSS MIKSAEKLDL
NLPLNLHLVN LVKCKRDSTI KRNVEYMGEG VGELCDWKEM IKLHQRQNGS LFDSPATTAA
ALIYHQHDQK CYQYLNSIFQ QHKNWVPTMY PTKVHSLLCL VDTLQNLGVH RHFKSEIKKA
LDEIYRLWQQ KNEQIFSNVT HCAMAFRLLR MSYYDVSSDE LAEFVDEEHF FATNGKYKSH
VEILELHKAS QLAIDHEKDD ILDKINNWTR AFMEQKLLNN GFIDRMSKKE VELALRKFYT
TSHLAENRRY IKSYEENNFK ILKAAYRSPN INNKDLLAFS IHDFELCQAQ HREELQQLKR
WFEDYRLDQL GLAERYIHAS YLFGVTVIPE PELSDARLMY AKYVMLLTIV DDHFESFASK
DECFNIIELV ERWDDYASVG YKSEKVKVFF SVFYKSIEEL ATIAEIKQGR SVKNHLINLW
LELMKLMLME RVEWCSGKTI PSIEEYLYVT SITFCAKLIP LSTQYFLGIK ISKDLLESDE
ICGLWNCSGR VMRILNDLQD SKREQKEVSI NLVTLLMKSM SEEEAIMKIK EILEMNRREL
LKMVLVQKKG SQLPQLCKDI FWRTSKWAHF TYSQTDGYRI AEEMKNHIDE VFYKPLNH
