ID   TPS2_MATCR              Reviewed;         546 AA.
AC   I6R4V5;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Alpha-isocomene synthase;
DE            EC=4.2.3.136;
DE   AltName: Full=Terpene synthase 2;
OS   Matricaria chamomilla var. recutita (German chamomile) (Chamomilla
OS   recutita).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC   Matricariinae; Matricaria.
OX   NCBI_TaxID=127986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Bodegold;
RX   PubMed=22682202; DOI=10.1186/1471-2229-12-84;
RA   Irmisch S., Krause S.T., Kunert G., Gershenzon J., Degenhardt J.,
RA   Koellner T.G.;
RT   "The organ-specific expression of terpene synthase genes contributes to the
RT   terpene hydrocarbon composition of chamomile essential oils.";
RL   BMC Plant Biol. 12:84-84(2012).
CC   -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of alpha-
CC       isocomene as the major product and detectable amounts of beta-
CC       caryophyllene, beta-isocomene, silphinene and modeph-2-ene. Produces
CC       exclusively the (-)-(E)-beta caryophyllene enantiomer.
CC       {ECO:0000269|PubMed:22682202}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (-)-alpha-isocomene +
CC         diphosphate; Xref=Rhea:RHEA:34699, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:68666, ChEBI:CHEBI:175763; EC=4.2.3.136;
CC         Evidence={ECO:0000269|PubMed:22682202};
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   -!- TISSUE SPECIFICITY: Highly expressed in roots, lower levels in stems
CC       and leaves and detected in disk florets, but not in ray florets.
CC       {ECO:0000269|PubMed:22682202}.
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. Tpsa subfamily.
CC       {ECO:0000305}.
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DR   EMBL; JQ255376; AFM43735.1; -; mRNA.
DR   AlphaFoldDB; I6R4V5; -.
DR   SMR; I6R4V5; -.
DR   PRIDE; I6R4V5; -.
DR   KEGG; ag:AFM43735; -.
DR   BRENDA; 4.2.3.136; 9733.
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; Manganese; Metal-binding.
FT   CHAIN           1..546
FT                   /note="Alpha-isocomene synthase"
FT                   /id="PRO_0000421926"
FT   MOTIF           299..303
FT                   /note="DDXXD motif"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         443
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   546 AA;  63446 MW;  A9AC736DF335AA5D CRC64;
     MSLQENVIRP TANFPPSVWG DQFLTYDERE DQAGLEKVVE DLKDKVRQEI LGTLDVPSQH
     TDLLRLIDSI QRLGIAYHFE EEIDRTLHHF YDAYGDNWTG GATSVWFRIM RQHGFFVSSD
     VFKSYKDKNG AFKEPLENDI VGFLELYEAT YLRVPGEVIL DDALVFTKGR LGEISNDPLW
     RNSIVSTQII EALEQPVQKR LHRHEALRYI TFYQQQASCN ESLLKLAKLG FNLLQSLHKK
     ELSQVYKWWK GFDVPTNLPY ARNRMVECYF WSLSVFFEPK YSESRMFLAK VFAVETILDD
     TYDAFGTYEE LEIFTAAVHR SSVTCLDALP KNYKLIYRII LSLYEDMEKI LTKMGKAHHL
     NYIRNAMMEY IGCYLKEAKW ANDEYTPTME EHKEVTTVSS GYKFSLIASF AAMGDAITDE
     TFKWALTMPP LAKACCVLCR VMDDIVTHKE EQERKHVASG IQCYMKEFDV TEQHVYDVFN
     AKVEDAWVEM NEESLKCKDV KRPVIMRVIN LARAMDVLYK NKDHYTHVGP ELINHIKSLV
     VDPIMA