ID   TPGD1_POGCB             Reviewed;         545 AA.
AC   Q49SP4;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   09-APR-2025, entry version 61.
DE   RecName: Full=Germacrene D synthase 1;
DE            EC=4.2.3.75;
DE   AltName: Full=PatTpsB15;
OS   Pogostemon cablin (Patchouli) (Mentha cablin).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Lamioideae; Pogostemoneae;
OC   Pogostemon.
OX   NCBI_TaxID=28511;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16970904; DOI=10.1016/j.abb.2006.08.006;
RA   Deguerry F., Pastore L., Wu S., Clark A., Chappell J., Schalk M.;
RT   "The diverse sesquiterpene profile of patchouli, Pogostemon cablin, is
RT   correlated with a limited number of sesquiterpene synthases.";
RL   Arch. Biochem. Biophys. 454:123-136(2006).
CC   -!- FUNCTION: Sesquiterpene synthase involved in germacrene D biosynthesis.
CC       Also produces at least 13 additional sesquiterpene products, including
CC       germacrene C and (+)-germacrene A, beta-ylangene, (E)-beta-farnesene
CC       and (E,E)-alpha-farnesene. {ECO:0000269|PubMed:16970904}.
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:16970904};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
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. {ECO:0000305}.
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DR   EMBL; AY508729; AAS86322.1; -; mRNA.
DR   AlphaFoldDB; Q49SP4; -.
DR   SMR; Q49SP4; -.
DR   BioCyc; MetaCyc:MONOMER-14835; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0052577; F:germacrene-D synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   GO; GO:0045338; P:farnesyl diphosphate metabolic process; IDA:UniProtKB.
DR   GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
DR   CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR   FunFam; 1.10.600.10:FF:000007; Isoprene synthase, chloroplastic; 1.
DR   FunFam; 1.50.10.130:FF:000001; Isoprene synthase, chloroplastic; 1.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR   Gene3D; 1.50.10.130; Terpene synthase, N-terminal domain; 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; IPR050148; Terpene_synthase-like.
DR   InterPro; IPR005630; Terpene_synthase_metal-bd.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR31225:SF93; ALPHA-HUMULENE_(-)-(E)-BETA-CARYOPHYLLENE SYNTHASE; 1.
DR   PANTHER; PTHR31225; OS04G0344100 PROTEIN-RELATED; 1.
DR   Pfam; PF01397; Terpene_synth; 1.
DR   Pfam; PF03936; Terpene_synth_C; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..545
FT                   /note="Germacrene D synthase 1"
FT                   /id="PRO_0000419751"
FT   MOTIF           298..302
FT                   /note="DDXXD motif"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
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   545 AA;  64197 MW;  C3B5D57EE67FBCC2 CRC64;
     MDLNEITSSS RPLANYHPNV WGDRFLLHEP EFTCQAGEKQ LVEELKEEVR RELKEASNDY
     LRQLKMVDAI QRLGIEYLFE EEIDEALRNL LAKFENYCKD NHDMYATALS FRLLRQHGYK
     VSCEVFDKFK DGEDGFKVEE VMAVLELFEA THMRIHGEDV LDQAFVFTRN YLQSIHATLS
     NPIAKQVHNA LNGYSCRRGM PRIEARKYIP IYEEYGCHHK ALLKLAKLDF NLLQSMHKRE
     LTQLYRWWKD LEMPTKLPYI RDRLVETYFW DMGFYFEPQY ALARNILVKV QCLVSIFDDT
     FDAYGAFKEL QLFKDAIDRW SISCLDELPE YMQIIYKLVL DVFEEIESHM IKQGTSYRLD
     YAREAIKIVI GGYFDEAKWR EEEYKPRMEE YMKVATKSAA YLTLIIVSFV GMKNDIATPQ
     AFQWVLSEPQ IITASLALAR LSNDLVGIEF EKERKYIATA VELYEEEHKV SKEEAVLELR
     HETESAWKEI NEALLEPTTF ATPILDRILN SARVLEVFYD KTDRYTHVDL ELQNIIAQLY
     IHPIP
//