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Myrcene synthase, chloroplastic (EC 4.2.3.15) (Monoterpene synthase MTS2) (HlMTS2)

 MTS2_HUMLU              Reviewed;         613 AA.
B6SCF4;
15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 1.
28-FEB-2018, entry version 35.
RecName: Full=Myrcene synthase, chloroplastic {ECO:0000305};
EC=4.2.3.15 {ECO:0000269|PubMed:18775972};
AltName: Full=Monoterpene synthase MTS2 {ECO:0000303|PubMed:18775972};
Short=HlMTS2 {ECO:0000303|PubMed:18775972};
Flags: Precursor;
Humulus lupulus (European hop).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Rosales; Cannabaceae; Humulus.
NCBI_TaxID=3486 {ECO:0000312|EMBL:ACI32638.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND TISSUE
SPECIFICITY.
TISSUE=Lupulin gland;
PubMed=18775972; DOI=10.1104/pp.108.125187;
Wang G., Tian L., Aziz N., Broun P., Dai X., He J., King A.,
Zhao P.X., Dixon R.A.;
"Terpene biosynthesis in glandular trichomes of hop.";
Plant Physiol. 148:1254-1266(2008).
-!- FUNCTION: Monoterpene synthase that catalyzes the formation of
myrcene. Can use geranyl diphosphate as substrate, but not
farnesyl diphosphate or geranylgeranyl diphosphate.
{ECO:0000269|PubMed:18775972}.
-!- CATALYTIC ACTIVITY: Geranyl diphosphate = myrcene + diphosphate.
{ECO:0000269|PubMed:18775972}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q40577};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.65 uM for geranyl diphosphate
{ECO:0000269|PubMed:18775972};
-!- PATHWAY: Secondary metabolite biosynthesis; terpenoid
biosynthesis.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000255};
Single-pass membrane protein {ECO:0000255}.
-!- TISSUE SPECIFICITY: Expressed in trichomes.
{ECO:0000269|PubMed:18775972}.
-!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important
for the catalytic activity, presumably through binding to Mg(2+).
{ECO:0000250|UniProtKB:Q40577}.
-!- SIMILARITY: Belongs to the terpene synthase family. Tpsb
subfamily. {ECO:0000305}.
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EMBL; EU760349; ACI32638.1; -; mRNA.
SMR; B6SCF4; -.
UniPathway; UPA00213; -.
GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0050551; F:myrcene synthase activity; IEA:UniProtKB-EC.
GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.600.10; -; 2.
Gene3D; 1.50.10.130; -; 1.
InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
InterPro; IPR034741; Terpene_cyclase_like_1_C.
InterPro; IPR001906; Terpene_synth_N.
InterPro; IPR036965; Terpene_synth_N_sf.
InterPro; IPR005630; Terpene_synthase_metal-bd.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
Pfam; PF01397; Terpene_synth; 1.
Pfam; PF03936; Terpene_synth_C; 1.
SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
SUPFAM; SSF48239; SSF48239; 1.
SUPFAM; SSF48576; SSF48576; 1.
1: Evidence at protein level;
Chloroplast; Lyase; Magnesium; Membrane; Metal-binding; Plastid;
Transit peptide; Transmembrane; Transmembrane helix.
TRANSIT 1 46 Chloroplast. {ECO:0000255}.
CHAIN 47 613 Myrcene synthase, chloroplastic.
{ECO:0000255}.
/FTId=PRO_0000439241.
TRANSMEM 455 475 Helical. {ECO:0000255}.
MOTIF 361 365 DDXXD motif. {ECO:0000305}.
METAL 361 361 Magnesium 1.
{ECO:0000250|UniProtKB:Q40577}.
METAL 361 361 Magnesium 2.
{ECO:0000250|UniProtKB:Q40577}.
METAL 365 365 Magnesium 1.
{ECO:0000250|UniProtKB:Q40577}.
METAL 365 365 Magnesium 2.
{ECO:0000250|UniProtKB:Q40577}.
METAL 506 506 Magnesium 3.
{ECO:0000250|UniProtKB:Q40577}.
METAL 510 510 Magnesium 3.
{ECO:0000250|UniProtKB:Q40577}.
METAL 514 514 Magnesium 3.
{ECO:0000250|UniProtKB:Q40577}.
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


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