ID   SELS_OCIBA              Reviewed;         550 AA.
AC   Q5SBP7;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Selinene synthase;
DE            EC=4.2.3.198 {ECO:0000269|PubMed:15516500};
GN   Name=SES;
OS   Ocimum basilicum (Sweet basil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Ociminae;
OC   Ocimum.
OX   NCBI_TaxID=39350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15516500; DOI=10.1104/pp.104.051318;
RA   Iijima Y., Davidovich-Rikanati R., Fridman E., Gang D.R., Bar E.,
RA   Lewinsohn E., Pichersky E.;
RT   "The biochemical and molecular basis for the divergent patterns in the
RT   biosynthesis of terpenes and phenylpropenes in the peltate glands of three
RT   cultivars of basil.";
RL   Plant Physiol. 136:3724-3736(2004).
CC   -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of
CC       alpha- and beta-selinene from trans,trans-farnesyl diphosphate (FPP).
CC       Produces also some nerolidol. {ECO:0000269|PubMed:15516500}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (+)-beta-selinene +
CC         diphosphate; Xref=Rhea:RHEA:29483, ChEBI:CHEBI:10443,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.198;
CC         Evidence={ECO:0000269|PubMed:15516500};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = alpha-selinene + diphosphate;
CC         Xref=Rhea:RHEA:47052, ChEBI:CHEBI:33019, ChEBI:CHEBI:59961,
CC         ChEBI:CHEBI:175763; EC=4.2.3.198;
CC         Evidence={ECO:0000269|PubMed:15516500};
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   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
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. {ECO:0000305}.
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DR   EMBL; AY693643; AAV63785.1; -; mRNA.
DR   AlphaFoldDB; Q5SBP7; -.
DR   SMR; Q5SBP7; -.
DR   PRIDE; Q5SBP7; -.
DR   KEGG; ag:AAV63785; -.
DR   BioCyc; MetaCyc:MON-14959; -.
DR   BRENDA; 4.2.3.198; 4385.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
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   Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..550
FT                   /note="Selinene synthase"
FT                   /id="PRO_0000399251"
FT   MOTIF           314..318
FT                   /note="DDXXD motif"
FT   BINDING         314
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         450
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         458
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   550 AA;  63125 MW;  C3A1ADC5A43E316B CRC64;
     MSANCVSAAP TSPKNSDVEE IRKSATYHSS VWGNHFLSYT SDVTEITAAE KEQLEKLKEK
     VKNLLAQTPD ESTGKMELID AIQRLGVGYH FTTEIQESLR QIHEGQIRND DDDVRVVALR
     FRLLRQGGYR APCDVFEKFM DDGGNFKESL KKDVEGMLSL YEASYYGIDG EEIMDKALEF
     SSSHLESMLH NISTKTNKSL LRRLQEALDT PISKAAIRLG ATKFISTYRE DESHNEDILN
     FAKLDFNILQ KMHQEEANYL TRWWEDLDLA SKLDFARDRM VESYFWSLGV YFQPQYRTSR
     IYLTKIISIV AVIDDIYDVY GSFDDLRSFT DVIQSWKISN ADELPPYMRI CFEALLGIYE
     DMGDRIGAPY AIDTMKELVD TYMQEAEWCY TEYVPTVDEY MKVALVTGGY LMVATTFLTG
     INNITKKDFD WIRNRPRLLQ VAEVLTRLMD DIAGHGTEKK TTAVSCYMKE YECSEMEASR
     ELSKQVKKAW KDLNDEWMEP RSSSAEIIGC IVNMSRVLHI MYSTGDDGFS DSSTRTTQAV
     KTLLVDHPMN