ID   TPS5_MATCR              Reviewed;         549 AA.
AC   I6QPS5;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=(-)-germacrene D synthase;
DE            EC=4.2.3.75;
DE   AltName: Full=Terpene synthase 5;
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 mainly in the biosynthesis of
CC       germacrene D. Produces exclusively the (-)-enantiomer.
CC       {ECO:0000269|PubMed:22682202}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (-)-germacrene D + diphosphate;
CC         Xref=Rhea:RHEA:12016, ChEBI:CHEBI:33019, ChEBI:CHEBI:49044,
CC         ChEBI:CHEBI:175763; EC=4.2.3.75;
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 leaves, stems and disk florets.
CC       Detected in roots. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JQ837261; AFM43738.1; -; mRNA.
DR   AlphaFoldDB; I6QPS5; -.
DR   SMR; I6QPS5; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0052577; F:germacrene-D synthase activity; IEA:RHEA.
DR   GO; GO:0000287; F:magnesium ion binding; 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..549
FT                   /note="(-)-germacrene D synthase"
FT                   /id="PRO_0000421929"
FT   MOTIF           300..304
FT                   /note="DDXXD motif"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         304
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         444
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         452
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   549 AA;  64220 MW;  57A9FB814081A4E9 CRC64;
     MASRENEIIR PKANFHPSVW GDQFLVYEEP EDQVEVEKMV EGLKEEVRKE IVVALDNPSK
     HTDLLVLINE VQRLGIAYYF EEEIERALKH IYDTYGDHWK GGSAPLWFRL LRKQGYYVSC
     DIFNQYKDNT GSFKESLTND VHGMLELYEA AYMRVHDEVI LDDAPVFTKT HLAKMLKDSL
     GYNPTLSKYI QDSLERPIRK RLPRVDALHY IPFYEQQVSH NKSLLKLSKL GFNLLQSMHK
     KELSELFKWW KHFDVEKNIP YMRNRFVENY FWALGAYFEP QYSRARIFLT KVFAFATMLD
     DTYDAYGVYK ELEIFTQAVE RWSLTCLDAL PEYMKLIYKE LLDLYEEMDD TMAKEGAPYH
     VKYAKEAMKE FIGSYMTEAR WKHEGYVPTT EEHKAVAFIS SGYKMLTIAS FVGMGDIASE
     DSFKWALSNP PLIKASCSIC RMMDDVVGHK EEKERVGGHV ASSVDSYMKQ HNVTEDHVYD
     LFNTLVEDAW KDLNRESLIC KEIPMVLKMR LINLTCFIDT LYKYEDTFTN VGPELIDCIK
     SHLVHAMSV