ID   MYRS_QUEIL              Reviewed;         597 AA.
AC   Q93X23;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Myrcene synthase, chloroplastic;
DE            EC=4.2.3.15;
DE   Flags: Precursor;
OS   Quercus ilex (Holly oak).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fagales; Fagaceae; Quercus.
OX   NCBI_TaxID=58334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Leaf;
RX   PubMed=11683887; DOI=10.1046/j.1432-1033.2001.02519.x;
RA   Fischbach R.J., Zimmer W., Schnitzler J.-P.;
RT   "Isolation and functional analysis of a cDNA encoding a myrcene synthase
RT   from holm oak (Quercus ilex L.).";
RL   Eur. J. Biochem. 268:5633-5638(2001).
CC   -!- FUNCTION: Involved in monoterpene (C10) biosynthesis. The major product
CC       is myrcene followed by minor amounts (1.2%) of the cyclic monoterpene
CC       limonene. {ECO:0000269|PubMed:11683887}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=84 uM for geranyl diphosphate {ECO:0000269|PubMed:11683887};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Active up to 55 degrees
CC         Celsius. {ECO:0000269|PubMed:11683887};
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   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AJ304839; CAC41012.1; -; mRNA.
DR   AlphaFoldDB; Q93X23; -.
DR   SMR; Q93X23; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; Manganese; Metal-binding; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..56
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..597
FT                   /note="Myrcene synthase, chloroplastic"
FT                   /id="PRO_5000067003"
FT   MOTIF           347..351
FT                   /note="DDXXD motif"
FT   BINDING         347
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         347
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         351
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         351
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         495
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         499
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   597 AA;  69660 MW;  0067E640A19179B8 CRC64;
     MALKLLTSLP MYNFSRVPVS SKDPILLVTS RTRNGYLARP VQCMVANKVS TSPDILRRSA
     NYQPSIWNHD YIESLRIEYV GETCTRQINV LKEQVRMMLH KVVNPLEQLE LIEILQRLGL
     SYHFEEEIKR ILDGVYNNDH GGDTWKAENL YATALKFRLL RQHGYSVSQE VFNSFKDERG
     SFKACLCEDT KGMLSLYEAS FFLIEGENIL EEARDFSTKH LEEYVKQNKE KNLATLVNHS
     LEFPLHWRMP RLEARWFINI YRHNQDVNPI LLEFAELDFN IVQAAHQADL KQVSTWWKST
     GLVENLSFAR DRPVENFFWT VGLIFQPQFG YCRRMFTKVF ALITTIDDVY DVYGTLDELE
     LFTDVVERWD INAMDQLPDY MKICFLTLHN SVNEMALDTM KEQRFHIIKY LKKAWVDLCR
     YYLVEAKWYS NKYRPSLQEY IENAWISIGA PTILVHAYFF VTNPITKEAL DCLEEYPNII
     RWSSIIARLA DDLGTSTDEL KRGDVPKAIQ CYMNETGASE EGAREYIKYL ISATWKKMNK
     DRAASSPFSH IFIEIALNLA RMAQCLYQHG DGHGLGNRET KDRILSLLIQ PIPLNKD