MTS2_HUMLU
ID MTS2_HUMLU Reviewed; 613 AA.
AC B6SCF4;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Myrcene synthase, chloroplastic {ECO:0000305};
DE EC=4.2.3.15 {ECO:0000269|PubMed:18775972};
DE AltName: Full=Monoterpene synthase MTS2 {ECO:0000303|PubMed:18775972};
DE Short=HlMTS2 {ECO:0000303|PubMed:18775972};
DE Flags: Precursor;
OS Humulus lupulus (European hop).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Humulus.
OX NCBI_TaxID=3486 {ECO:0000312|EMBL:ACI32638.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lupulin gland;
RX PubMed=18775972; DOI=10.1104/pp.108.125187;
RA Wang G., Tian L., Aziz N., Broun P., Dai X., He J., King A., Zhao P.X.,
RA Dixon R.A.;
RT "Terpene biosynthesis in glandular trichomes of hop.";
RL Plant Physiol. 148:1254-1266(2008).
CC -!- FUNCTION: Monoterpene synthase that catalyzes the formation of myrcene.
CC Can use geranyl diphosphate as substrate, but not farnesyl diphosphate
CC or geranylgeranyl diphosphate. {ECO:0000269|PubMed:18775972}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.15;
CC Evidence={ECO:0000269|PubMed:18775972};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.65 uM for geranyl diphosphate {ECO:0000269|PubMed:18775972};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000255};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in trichomes.
CC {ECO:0000269|PubMed:18775972}.
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|UniProtKB:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
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DR EMBL; EU760349; ACI32638.1; -; mRNA.
DR AlphaFoldDB; B6SCF4; -.
DR SMR; B6SCF4; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050551; F:myrcene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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; Membrane; Metal-binding; Plastid;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..613
FT /note="Myrcene synthase, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439241"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 361..365
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 361
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 365
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 365
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 506
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 510
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 514
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 613 AA; 72214 MW; 1018922AF9DA9B2A CRC64;
MQCMAVHQFA PLLSLLNCSR ISSDFGRLFT PKTSTKSRSS TCHPIQCTVV NNTDRRSANY
EPSIWSFDYI QSLTSQYKGK SYSSRLNELK KEVKMMEDGT KECLAQLDLI DTLQRLGISY
HFEDEINTIL KRKYINIQNN INHNYNLYST ALQFRLLRQH GYLVTQEVFN AFKDETGKFK
TYLSDDIMGV LSLYEASFYA MKHENVLEEA RVFSTECLKE YMMKMEQNKV LLDHDLDHND
NFNVNHHVLI INHALELPLH WRITRSEARW FIDVYEKKQD MDSTLLEFAK LDFNMVQSTH
QEDLKHLSRW WRHSKLGEKL NFARDRLMEA FLWEVGLKFE PEFSYFKRIS ARLFVLITII
DDIYDVYGTL EELELFTKAV ERWDVNAINE LPEYMKMPFL VLHNTINEMA FDVLGDQNFL
NIEYLKKSLV DLCKCYLQEA KWYYSGYQPT LQEYIEMAWL SIGGPVILVH AYFCFTNPIT
KESMKFFTEG YPNIIQQSCL IVRLADDFGT FSDELNRGDV PKSIQCYMYD TGASEDEARE
HIKFLICETW KDMNKNDEDN SCFSETFVEV CKNLARTALF MYQYGDGHAS QNCLSKERIF
ALIINPINFH ERK
