ID   TPGD2_POGCB             Reviewed;         554 AA.
AC   Q49SP6;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Germacrene D synthase 2;
DE            EC=4.2.3.75;
DE   AltName: Full=PatTpsBF2;
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       {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; AY508727; AAS86320.1; -; mRNA.
DR   AlphaFoldDB; Q49SP6; -.
DR   SMR; Q49SP6; -.
DR   BioCyc; MetaCyc:MON-14836; -.
DR   BRENDA; 4.2.3.22; 9724.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0052577; F:germacrene-D synthase activity; IEA:RHEA.
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   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   Cytoplasm; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..554
FT                   /note="Germacrene D synthase 2"
FT                   /id="PRO_0000419752"
FT   MOTIF           307..311
FT                   /note="DDXXD motif"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
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"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   554 AA;  64149 MW;  86825F6DC59E5F86 CRC64;
     MELKNQSVAI ISSNASRPLA HYHPDVWGDR FLLYKPNPSS EAGQKPVIEE LKQQVRSELK
     EASNDYMRQL KMVDAIQRLG IESLFEEDID NALKNLSENF DDYCKDKHDL YAIALSFRLL
     RQHGYRISCD VFDKLKDGED GFKVPPSDEA LAVVELLEAT HLRIHGEVVL DRAFVFARIH
     LESIEANLNN PVAKQVHNAL YGYSNRRGMQ QVEARKYIPI YEQYASHHQG LLKLATLNFN
     LQQTMHKREL SELSRWYRDL EVPTMLPFAR QRLVETYFWD AGVVFEPEND VARMILVKVQ
     CLISFLDDTF DAYGSFEELQ LFTDAINTWD VSCLDQLPDY MKIIYKALLG VFEVIEKLMI
     KQGTLYRLNY AKEAMKIVVG GYFVEAKWRE EKSKPTTQEY MQVATKSAGY MTLIITSFLG
     MEANIATKEA FDWVLSEPDV MKAAITLARL TNDIVGIELE KERKHIATAV EVYEDEHKLS
     MQEAMVEIKN QIESGWKTIN EAFLRPTKFP TPILYRILNY CRVLEVIYDK SDRYTHVDPA
     LQDIIKQLYI HPIP